메뉴 건너뛰기




Volumn 89, Issue 2, 2011, Pages 87-97

TonB or not TonB: Is that the question?

Author keywords

Colicin; Iron; Protein structure; Siderophores; TonB

Indexed keywords

ACTIVE TRANSPORT; ATP-BINDING CASSETTE TRANSPORTERS; BACTERIAL CELLS; BINDING PROTEINS; COLICINS; CURRENT MODELS; CYTOPLASMIC MEMBRANE; ENERGY TRANSDUCTION; INNER MEMBRANES; IRON CHELATORS; IRON SOURCES; LACTOFERRIN; LOW MOLECULAR WEIGHT; NICKEL COMPLEX; OUTER MEMBRANE; PROTEIN STRUCTURE; SIDEROPHORES; THREE-DIMENSIONAL STRUCTURE; TONB; VITAMIN B12;

EID: 78651364685     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O10-141     Document Type: Review
Times cited : (144)

References (98)
  • 1
    • 77953253806 scopus 로고    scopus 로고
    • The lactoferrin receptor complex in gram negative bacteria
    • doi:10.1007/s10534-010-9299-z. PMID:20155302
    • Beddek, A.J., and Schryvers, A.B. 2010. The lactoferrin receptor complex in gram negative bacteria. Biometals, 23(3): 377-386. doi:10.1007/s10534-010- 9299-z. PMID:20155302.
    • (2010) Biometals , vol.23 , Issue.3 , pp. 377-386
    • Beddek, A.J.1    Schryvers, A.B.2
  • 2
    • 45649085030 scopus 로고    scopus 로고
    • Plant carbohydrate scavenging through TonB-dependent receptors: A feature shared by phytopathogenic and aquatic bacteria
    • doi:10.1371/journal. pone.0000224. PMID:17311090
    • Blanvillain, S., Meyer, D., Boulanger, A., Lautier, M., Guynet, C., Denance, N., et al. 2007. Plant carbohydrate scavenging through TonB-dependent receptors: a feature shared by phytopathogenic and aquatic bacteria. PLoS One, 2(2): e224. doi:10.1371/journal. pone.0000224. PMID:17311090.
    • (2007) PLoS One , vol.2 , Issue.2
    • Blanvillain, S.1    Meyer, D.2    Boulanger, A.3    Lautier, M.4    Guynet, C.5    Denance, N.6
  • 3
    • 0027280517 scopus 로고
    • The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli
    • Bradbeer, C. 1993. The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli. J. Bacteriol. 175(10): 3146-3150. PMID:8387997. (Pubitemid 23148752)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 3146-3150
    • Bradbeer, C.1
  • 4
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • DOI 10.1016/S0300-9084(02)01427-X, PII S030090840201427X
    • Braun, V., Patzer, S.I., and Hantke, K. 2002. Ton-dependent colicins and microcins: modular design and evolution. Biochimie, 84(5-6): 365-380. doi:10.1016/S0300-9084(02)01427-X. PMID:12423780. (Pubitemid 35350867)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 5
    • 0042838110 scopus 로고    scopus 로고
    • In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12
    • DOI 10.1128/JB.185.18.5508-5518.2003
    • Braun, M., Endriss, F., Killmann, H., and Braun, V. 2003. In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12. J. Bacteriol. 185(18): 5508-5518. doi:10.1128/JB.185.18. 5508-5518.2003. PMID:12949103. (Pubitemid 37082408)
    • (2003) Journal of Bacteriology , vol.185 , Issue.18 , pp. 5508-5518
    • Braun, M.1    Endriss, F.2    Killmann, H.3    Braun, V.4
  • 7
    • 34249095469 scopus 로고    scopus 로고
    • Structure of colicin I receptor bound to the R-domain of colicin Ia: Implications for protein import
    • DOI 10.1038/sj.emboj.7601693, PII 7601693
    • Buchanan, S.K., Lukacik, P., Grizot, S., Ghirlando, R., Ali, M.M., Barnard, T.J., et al. 2007. Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. EMBO J. 26(10): 2594-2604. doi:10.1038/sj.emboj.7601693. PMID:17464289. (Pubitemid 46788319)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2594-2604
    • Buchanan, S.K.1    Lukacik, P.2    Grizot, S.3    Ghirlando, R.4    Ali, M.M.U.5    Barnard, T.J.6    Jakes, K.S.7    Kienker, P.K.8    Esser, L.9
  • 8
    • 0032849375 scopus 로고    scopus 로고
    • Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter
    • DOI 10.1073/pnas.96.19.10673
    • Cadieux, N., and Kadner, R.J. 1999. Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter. Proc. Natl. Acad. Sci. U.S.A. 96(19): 10673-10678. doi:10.1073/pnas.96.19.10673.PMID:10485884. (Pubitemid 29442202)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.19 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 9
    • 0033764762 scopus 로고    scopus 로고
    • Sequence changes in the Ton box region of BtuB affect its transport activities and interaction with TonB protein
    • doi:10.1128/JB.182.21.5954-5961.2000. PMID:11029413
    • Cadieux, N., Bradbeer, C., and Kadner, R.J. 2000. Sequence changes in the Ton box region of BtuB affect its transport activities and interaction with TonB protein. J. Bacteriol. 182(21): 5954-5961. doi:10.1128/JB.182.21.5954-5961. 2000. PMID:11029413.
    • (2000) J. Bacteriol. , vol.182 , Issue.21 , pp. 5954-5961
    • Cadieux, N.1    Bradbeer, C.2    Kadner, R.J.3
  • 12
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB
    • DOI 10.1046/j.1365-2958.2001.02673.x
    • Cascales, E., Lloubes, R., and Sturgis, J.N. 2001. The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB. Mol. Microbiol. 42(3): 795-807. doi:10.1046/j.1365-2958.2001.02673.x. PMID:11722743. (Pubitemid 33064487)
    • (2001) Molecular Microbiology , vol.42 , Issue.3 , pp. 795-807
    • Cascales, E.1    Lloubes, R.2    Sturgis, J.N.3
  • 14
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
    • doi:10.1074/jbc.M102778200. PMID:11328822
    • Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. 2001. Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold. J. Biol. Chem. 276(29): 27535-27540. doi:10.1074/jbc.M102778200. PMID:11328822.
    • (2001) J. Biol. Chem. , vol.276 , Issue.29 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Pluckthun, A.3    Wlodawer, A.4
  • 15
    • 33750965918 scopus 로고    scopus 로고
    • In Meso Structure of the Cobalamin Transporter, BtuB, at 1.95 A Resolution
    • DOI 10.1016/j.jmb.2006.09.022, PII S0022283606012113
    • Cherezov, V., Yamashita, E., Liu, W., Zhalnina, M., Cramer, W.A., and Caffrey, M. 2006. In meso structure of the cobalamin transporter, BtuB, at 1.95 A resolution. J. Mol. Biol. 364(4): 716-734. doi:10.1016/j.jmb.2006.09.022. PMID:17028020. (Pubitemid 44737826)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.4 , pp. 716-734
    • Cherezov, V.1    Yamashita, E.2    Liu, W.3    Zhalnina, M.4    Cramer, W.A.5    Caffrey, M.6
  • 16
    • 0041384402 scopus 로고    scopus 로고
    • The Escherichia coli outer membrane cobalamin transporter BtuB: Structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation
    • DOI 10.1016/j.jmb.2003.07.005
    • Chimento, D.P., Kadner, R.J., and Wiener, M.C. 2003. The Escher-ichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation. J. Mol. Biol. 332(5): 999-1014. doi:10.1016/j. jmb.2003.07.005. PMID:14499604. (Pubitemid 37108794)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.5 , pp. 999-1014
    • Chimento, D.P.1    Kadner, R.J.2    Wiener, M.C.3
  • 17
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: Implications for the transport cycle
    • DOI 10.1002/prot.20416
    • Chimento, D.P., Kadner, R.J., and Wiener, M.C. 2005. Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins, 59(2): 240-251. doi:10.1002/prot.20416. PMID:15739205. (Pubitemid 40471563)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.2 , pp. 240-251
    • Chimento, D.P.1    Kadner, R.J.2    Wiener, M.C.3
  • 18
    • 34248636774 scopus 로고    scopus 로고
    • Bioinformatic analysis of the TonB protein family
    • DOI 10.1007/s10534-006-9049-4, Biometals: function and transport in bacteria, fungi, and humans
    • Chu, B.C., Peacock, R.S., and Vogel, H.J. 2007. Bioinformatic analysis of the TonB protein family. Biometals, 20(3): 467-483. doi:10.1007/s10534-006- 9049-4. PMID:17225063. (Pubitemid 46776564)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 467-483
    • Chu, B.C.H.1    Peacock, R.S.2    Vogel, H.J.3
  • 19
    • 24644432870 scopus 로고    scopus 로고
    • Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa
    • DOI 10.1016/j.jmb.2005.08.004, PII S0022283605009046
    • Cobessi, D., Celia, H., and Pattus, F. 2005. Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J. Mol. Biol. 352(4): 893-904. doi:10.1016/j.jmb.2005.08.004. PMID:16139844. (Pubitemid 41267075)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.4 , pp. 893-904
    • Cobessi, D.1    Celia, H.2    Pattus, F.3
  • 20
    • 77449152698 scopus 로고    scopus 로고
    • 2010. Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: Heme binding by an induced fit mechanism
    • doi:10.1002/prot.22539. PMID:19731368
    • Cobessi, D., Meksem, A., and Brillet, K. 2010. Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: heme binding by an induced fit mechanism. Proteins, 78(2): 286-294. doi:10.1002/prot.22539. PMID:19731368.
    • Proteins , vol.78 , Issue.2 , pp. 286-294
    • Cobessi, D.1    Meksem, A.2    Brillet, K.3
  • 21
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram- negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • DOI 10.1111/j.1365-2958.1994.tb01021.x
    • De Mot, R., and Vanderleyden, J. 1994. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol. Microbiol. 12(2): 333-334. doi:10.1111/j.1365-2958.1994.tb01021.x. PMID:8057857. (Pubitemid 24197488)
    • (1994) Molecular Microbiology , vol.12 , Issue.2 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 22
    • 0014976040 scopus 로고
    • Fine structure and isolation of the hook-basal body complex of flagella from Escherichia coli and Bacillus subtilis
    • PMID:4993325
    • DePamphilis, M.L., and Adler, J. 1971. Fine structure and isolation of the hook-basal body complex of flagella from Escherichia coli and Bacillus subtilis. J. Bacteriol. 105(1): 384-395. PMID:4993325.
    • (1971) J. Bacteriol. , vol.105 , Issue.1 , pp. 384-395
    • Depamphilis, M.L.1    Adler, J.2
  • 23
    • 34447339934 scopus 로고    scopus 로고
    • Studies on colicin B translocation: FepA is gated by TonB
    • DOI 10.1111/j.1365-2958.2007.05808.x
    • Devanathan, S., and Postle, K. 2007. Studies on colicin B translocation: FepA is gated by TonB. Mol. Microbiol. 65(2): 441-453. doi:10.1111/j.1365-2958. 2007.05808.x. PMID:17578453. (Pubitemid 47052733)
    • (2007) Molecular Microbiology , vol.65 , Issue.2 , pp. 441-453
    • Devanathan, S.1    Postle, K.2
  • 24
    • 0020560565 scopus 로고
    • Electron microscopy of frozen-hydrated bacteria
    • Dubochet, J., McDowall, A.W., Menge, B., Schmid, E.N., and Lickfeld, K.G. 1983. Electron microscopy of frozen-hydrated bacteria. J. Bacteriol. 155(1): 381-390. PMID:6408064. (Pubitemid 13070635)
    • (1983) Journal of Bacteriology , vol.155 , Issue.1 , pp. 381-390
    • Dubochet, J.1    McDowall, A.W.2    Menge, B.3
  • 25
    • 0031569354 scopus 로고    scopus 로고
    • A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1
    • Elkins, P., Bunker, A., Cramer, W.A., and Stauffacher, C.V. 1997. A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1. Structure, 5(3): 443-458. doi:10.1016/S0969-2126(97) 00200-1. PMID:9083117. (Pubitemid 27169944)
    • (1997) Structure , vol.5 , Issue.3 , pp. 443-458
    • Elkins, P.1    Bunker, A.2    Cramer, W.A.3    Stauffacher, C.V.4
  • 26
    • 0242569215 scopus 로고    scopus 로고
    • Spectroscopic Evidence that Osmolytes Used in Crystallization Buffers Inhibit a Conformation Change in a Membrane Protein
    • DOI 10.1021/bi035439t
    • Fanucci, G.E., Lee, J.Y., and Cafiso, D.S. 2003. Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein. Biochemistry, 42(45): 13106-13112. doi:10.1021/bi035439t. PMID:14609320. (Pubitemid 37420662)
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13106-13112
    • Fanucci, G.E.1    Lee, J.Y.2    Cafiso, D.S.3
  • 27
    • 0842329749 scopus 로고    scopus 로고
    • Metal Import through Microbial Membranes
    • DOI 10.1016/S0092-8674(03)01030-4
    • Ferguson, A.D., and Deisenhofer, J. 2004. Metal import through microbial membranes. Cell, 116(1): 15-24. doi:10.1016/S00928674(03)01030-4. PMID:14718163. (Pubitemid 38165323)
    • (2004) Cell , vol.116 , Issue.1 , pp. 15-24
    • Ferguson, A.D.1    Deisenhofer, J.2
  • 28
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • DOI 10.1126/science.282.5397.2215
    • Ferguson, A.D., Hofmann, E., Coulton, J.W., Diederichs, K., and Welte, W. 1998. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science, 282(5397): 2215-2220. doi:10.1126/science.282. 5397.2215. PMID:9856937. (Pubitemid 29004062)
    • (1998) Science , vol.282 , Issue.5397 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 29
    • 0034079929 scopus 로고    scopus 로고
    • Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA
    • Ferguson, A.D., Coulton, J.W., Diederichs, K., Welte, W., Braun, V., and Fiedler, H.P. 2000. Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Protein Sci. 9(5): 956-963. doi:10.1110/ps.9.5.956. PMID:10850805. (Pubitemid 30353337)
    • (2000) Protein Science , vol.9 , Issue.5 , pp. 956-963
    • Ferguson, A.D.1    Braun, V.2    Fiedler, H.-P.3    Coulton, J.W.4    Diederichs, K.5    Welte, W.6
  • 30
    • 0034886699 scopus 로고    scopus 로고
    • Active transport of an antibiotic rifamycin derivative by the outer-membrane protein FhuA
    • DOI 10.1016/S0969-2126(01)00631-1, PII S0969212601006311
    • Ferguson, A.D., Kodding, J., Walker, G., Bos, C., Coulton, J.W., Diederichs, K., et al. 2001. Active transport of an antibiotic rifamycin derivative by the outer-membrane protein FhuA. Structure, 9(8): 707-716. doi:10.1016/S0969-2126(01)00631-1. PMID:11587645. (Pubitemid 32772893)
    • (2001) Structure , vol.9 , Issue.8 , pp. 707-716
    • Ferguson, A.D.1    Kodding, J.2    Walker, G.3    Bos, C.4    Coulton, J.W.5    Diederichs, K.6    Braun, V.7    Welte, W.8
  • 31
    • 57749083521 scopus 로고    scopus 로고
    • Molecular organization of Gram-negative peptidoglycan
    • doi:10.1073/pnas.0808035105. PMID:19033194
    • Gan, L., Chen, S., and Jensen, G.J. 2008. Molecular organization of Gram-negative peptidoglycan. Proc. Natl. Acad. Sci. U.S.A. 105(48): 18953-18957. doi:10.1073/pnas.0808035105. PMID:19033194.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.48 , pp. 18953-18957
    • Gan, L.1    Chen, S.2    Jensen, G.J.3
  • 32
    • 35748976227 scopus 로고    scopus 로고
    • The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins
    • DOI 10.1111/j.1365-2958.2007.05957.x
    • Garcia-Herrero, A., Peacock, R.S., Howard, S.P., and Vogel, H.J. 2007. The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins. Mol. Microbiol. 66(4): 872-889. doi:10.1111/j.1365-2958.2007.05957.x. PMID:17927700. (Pubitemid 350050416)
    • (2007) Molecular Microbiology , vol.66 , Issue.4 , pp. 872-889
    • Garcia-Herrero, A.1    Peacock, R.S.2    Howard, S.P.3    Vogel, H.J.4
  • 33
    • 0026071729 scopus 로고
    • Freeze-substitution of gram-negative eubacteria: General cell morphology and envelope profiles
    • PMID:1999383
    • Graham, L.L., Harris, R., Villiger, W., and Beveridge, T.J. 1991. Freeze-substitution of gram-negative eubacteria: general cell morphology and envelope profiles. J. Bacteriol. 173(5): 1623-1633. PMID:1999383.
    • (1991) J. Bacteriol. , vol.173 , Issue.5 , pp. 1623-1633
    • Graham, L.L.1    Harris, R.2    Villiger, W.3    Beveridge, T.J.4
  • 34
    • 34447339675 scopus 로고    scopus 로고
    • Mechanics of force propagation in TonB-dependent outer membrane transport
    • DOI 10.1529/biophysj.107.104158
    • Gumbart, J., Wiener, M.C., and Tajkhorshid, E. 2007. Mechanics of force propagation in TonB-dependent outer membrane transport. Biophys. J. 93(2): 496-504. doi:10.1529/biophysj.107. 104158. PMID:17449669. (Pubitemid 47057815)
    • (2007) Biophysical Journal , vol.93 , Issue.2 , pp. 496-504
    • Gumbart, J.1    Wiener, M.C.2    Tajkhorshid, E.3
  • 35
    • 0025599473 scopus 로고
    • TonB protein of Salmonella typhimurium. A model for signal transduction between membranes
    • doi:10.1016/S00222836(99)80009-6. PMID:2266561
    • Hannavy, K., Barr, G.C., Dorman, C.J., Adamson, J., Mazengera, L.R., Gallagher, M.P., et al. 1990. TonB protein of Salmonella typhimurium. A model for signal transduction between membranes. J. Mol. Biol. 216(4): 897-910. doi:10.1016/S00222836(99)80009-6. PMID:2266561.
    • (1990) J. Mol. Biol. , vol.216 , Issue.4 , pp. 897-910
    • Hannavy, K.1    Barr, G.C.2    Dorman, C.J.3    Adamson, J.4    Mazengera, L.R.5    Gallagher, M.P.6
  • 36
    • 1242297815 scopus 로고    scopus 로고
    • Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution
    • DOI 10.1111/j.1365-2958.2003.03884.x
    • Hilsenbeck, J.L., Park, H., Chen, G., Youn, B., Postle, K., and Kang, C. 2004. Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution. Mol. Microbiol. 51(3): 711-720. doi:10.1111/j.1365-2958.2003.03884. x. PMID:14731273. (Pubitemid 38233938)
    • (2004) Molecular Microbiology , vol.51 , Issue.3 , pp. 711-720
    • Hilsenbeck, J.L.1    Park, H.2    Chen, G.3    Youn, B.4    Postle, K.5    Kang, C.6
  • 37
    • 68649085420 scopus 로고    scopus 로고
    • The peptidoglycan-binding (PGB) domain of the Escherichia coli Pal protein can also function as the PGB domain in E. coli flagellar motor protein MotB
    • doi:10.1093/jb/mvp061. PMID:19364805
    • Hizukuri, Y., Morton, J.F., Yakushi, T., Kojima, S., and Homma, M. 2009. The peptidoglycan-binding (PGB) domain of the Escherichia coli Pal protein can also function as the PGB domain in E. coli flagellar motor protein MotB. J. Biochem. 146(2): 219-229. doi:10.1093/jb/mvp061. PMID:19364805.
    • (2009) J. Biochem. , vol.146 , Issue.2 , pp. 219-229
    • Hizukuri, Y.1    Morton, J.F.2    Yakushi, T.3    Kojima, S.4    Homma, M.5
  • 38
    • 0021134178 scopus 로고
    • Periplasmic gel: New concept resulting from the reinvestigation of bacterial cell envelope ultrastructure by new methods
    • Hobot, J.A., Carlemalm, E., Villiger, W., and Kellenberger, E. 1984. Periplasmic gel: new concept resulting from the reinvestigation of bacterial cell envelope ultrastructure by new methods. J. Bacteriol. 160(1): 143-152. PMID:6207168. (Pubitemid 14022809)
    • (1984) Journal of Bacteriology , vol.160 , Issue.1 , pp. 143-152
    • Hobot, J.A.1    Carlemalm, E.2    Villiger, W.3    Kellenberger, E.4
  • 39
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • DOI 10.1111/j.1365-2958.2008.06327.x
    • Hullmann, J., Patzer, S.I., Romer, C., Hantke, K., and Braun, V. 2008. Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol. Microbiol. 69(4): 926-937. doi:10.1111/j. 1365-2958.2008.06327.x. PMID:18554332. (Pubitemid 352033311)
    • (2008) Molecular Microbiology , vol.69 , Issue.4 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Romer, C.3    Hantke, K.4    Braun, V.5
  • 40
    • 75149196290 scopus 로고    scopus 로고
    • The colicin Ia receptor, Cir, is also the translocator for colicin Ia
    • doi:10.1111/j.1365-2958.2009.06966.x. PMID:19919671
    • Jakes, K.S., and Finkelstein, A. 2010. The colicin Ia receptor, Cir, is also the translocator for colicin Ia. Mol. Microbiol. 75(3): 567-578. doi:10.1111/j.1365-2958.2009.06966.x. PMID:19919671.
    • (2010) Mol. Microbiol , vol.75 , Issue.3 , pp. 567-578
    • Jakes, K.S.1    Finkelstein, A.2
  • 41
    • 0036589253 scopus 로고    scopus 로고
    • Killing of E. coli cells by E group nuclease colicins
    • DOI 10.1016/S0300-9084(02)01450-5, PII S0300908402014505
    • James, R., Penfold, C.N., Moore, G.R., and Kleanthous, C. 2002. Killing of E. coli cells by E group nuclease colicins. Biochimie, 84(5-6): 381-389. doi:10.1016/S0300-9084(02)01450-5. PMID:12423781 (Pubitemid 35350868)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 381-389
    • James, R.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4
  • 42
    • 70349629987 scopus 로고    scopus 로고
    • TonB interacts with BtuF, the Escherichia coli periplasmic binding protein for cyanocobalamin
    • doi:10.1021/bi900722p. PMID:19708689
    • James, K.J., Hancock, M.A., Gagnon, J.N., and Coulton, J.W. 2009. TonB interacts with BtuF, the Escherichia coli periplasmic binding protein for cyanocobalamin. Biochemistry, 48(39): 9212-9220. doi:10.1021/bi900722p. PMID:19708689.
    • (2009) Biochemistry , vol.48 , Issue.39 , pp. 9212-9220
    • James, K.J.1    Hancock, M.A.2    Gagnon, J.N.3    Coulton, J.W.4
  • 43
    • 0026723111 scopus 로고
    • Membrane topology of the Escherichia coli ExbD protein
    • PMID:1644779
    • Kampfenkel, K., and Braun, V. 1992. Membrane topology of the Escherichia coli ExbD protein. J. Bacteriol. 174(16): 5485-5487. PMID:1644779.
    • (1992) J. Bacteriol. , vol.174 , Issue.16 , pp. 5485-5487
    • Kampfenkel, K.1    Braun, V.2
  • 44
    • 0027466914 scopus 로고
    • Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli
    • Kampfenkel, K., and Braun, V. 1993. Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 268(8): 6050-6057. PMID:8449962. (Pubitemid 23090944)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.8 , pp. 6050-6057
    • Kampfenkel, K.1    Braun, V.2
  • 45
    • 0027238302 scopus 로고
    • ExbB acts as a chaperone-like protein to stabilize TonB in the cytoplasm
    • Karlsson, M., Hannavy, K., and Higgins, C.F. 1993. ExbB acts as a chaperone-like protein to stabilize TonB in the cytoplasm. Mol. Microbiol. 8(2): 389-396. doi:10.1111/j.1365-2958.1993. tb01582.x. PMID:8100348. (Pubitemid 23124555)
    • (1993) Molecular Microbiology , vol.8 , Issue.2 , pp. 389-396
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 46
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • DOI 10.1074/jbc.M212239200
    • Karpowich, N.K., Huang, H.H., Smith, P.C., and Hunt, J.F. 2003. Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding. J. Biol. Chem. 278(10): 8429-8434. doi:10.1074/jbc.M212239200. PMID:12468528. (Pubitemid 36800593)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 47
    • 0036842863 scopus 로고    scopus 로고
    • Demonstration and characterization of a specific interaction between gonococcal transferrin binding protein A and TonB
    • DOI 10.1128/JB.184.22.6138-6145.2002
    • Kenney, C.D., and Cornelissen, C.N. 2002. Demonstration and characterization of a specific interaction between gonococcal transferrin binding protein A and TonB. J. Bacteriol. 184(22): 6138-6145. doi:10.1128/JB.184.22.6138-6145.2002. PMID:12399483. (Pubitemid 35265894)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6138-6145
    • Kenney, C.D.1    Cornelissen, C.N.2
  • 48
    • 0028942302 scopus 로고
    • Identification of receptor binding sites by competitive peptide mapping: Phages T1, T5, and 80 and colicin M bind to the gating loop of FhuA
    • PMID:7836303
    • Killmann, H., Videnov, G., Jung, G., Schwarz, H., and Braun, V. 1995. Identification of receptor binding sites by competitive peptide mapping: phages T1, T5, and 80 and colicin M bind to the gating loop of FhuA. J. Bacteriol. 177(3): 694-698. PMID:7836303.
    • (1995) J. Bacteriol. , vol.177 , Issue.3 , pp. 694-698
    • Killmann, H.1    Videnov, G.2    Jung, G.3    Schwarz, H.4    Braun, V.5
  • 49
    • 13244255594 scopus 로고    scopus 로고
    • Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments
    • DOI 10.1074/jbc.M411155200
    • Kodding, J., Killig, F., Polzer, P., Howard, S.P., Diederichs, K., and Welte, W. 2005. Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments. J. Biol. Chem. 280(4): 3022-3028. doi:10.1074/jbc. M411155200. PMID:15522863. (Pubitemid 40189412)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 3022-3028
    • Kodding, J.1    Killig, F.2    Polzer, P.3    Howard, S.P.4    Diederichs, K.5    Welte, W.6
  • 50
    • 1642287423 scopus 로고    scopus 로고
    • Dimerization of TonB Is Not Essential for Its Binding to the Outer Membrane Siderophore Receptor FhuA of Escherichia coli
    • DOI 10.1074/jbc.M311720200
    • Kodding, J., Howard, P., Kaufmann, L., Polzer, P., Lustig, A., and Welte, W. 2004. Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli. J. Biol. Chem. 279(11): 9978-9986. doi:10. 1074/jbc.M311720200. PMID:14665631. (Pubitemid 38372600)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 9978-9986
    • Koedding, J.1    Howard, P.2    Kaufmann, L.3    Polzer, P.4    Lustig, A.5    Welte, W.6
  • 51
    • 77950282521 scopus 로고    scopus 로고
    • The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria
    • doi:10.1002/pro.345. PMID:20095050
    • Kohler, S.D., Weber, A., Howard, S.P., Welte, W., and Drescher, M. 2010. The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria. Protein Sci. 19(4): 625-630. doi:10.1002/pro.345. PMID:20095050.
    • (2010) Protein Sci. , vol.19 , Issue.4 , pp. 625-630
    • Kohler, S.D.1    Weber, A.2    Howard, S.P.3    Welte, W.4    Drescher, M.5
  • 52
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R., Billeter, M., and Wuthrich, K. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14(1): 51-55. doi:10.1016/0263-7855(96)00009-4. PMID:8744573. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 54
    • 0030911410 scopus 로고    scopus 로고
    • Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
    • Larsen, R.A., Foster-Hartnett, D., McIntosh, M.A., and Postle, K. 1997. Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions. J. Bacteriol. 179(10): 3213-3221. PMID:9150216. (Pubitemid 27202995)
    • (1997) Journal of Bacteriology , vol.179 , Issue.10 , pp. 3213-3221
    • Larsen, R.A.1    Foster-Hartnett, D.2    McIntosh, M.A.3    Postle, K.4
  • 55
    • 0038385104 scopus 로고    scopus 로고
    • In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli
    • DOI 10.1046/j.1365-2958.2003.03579.x
    • Larsen, R.A., Letain, T.E., and Postle, K. 2003. In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli. Mol. Microbiol. 49(1): 211-218. doi:10.1046/j. 1365-2958.2003.03579.X. PMID:12823822. (Pubitemid 36792015)
    • (2003) Molecular Microbiology , vol.49 , Issue.1 , pp. 211-218
    • Larsen, R.A.1    Letain, T.E.2    Postle, K.3
  • 56
    • 0021946983 scopus 로고
    • Correlation between degradation and ultrastructure of peptidoglycan during autolysis of Escherichia coli
    • Leduc, M., Frehel, C., and van Heijenoort, J. 1985. Correlation between degradation and ultrastructure of peptidoglycan during autolysis of Escherichia coli. J. Bacteriol. 161(2): 627-635. PMID:3918020. (Pubitemid 15168922)
    • (1985) Journal of Bacteriology , vol.161 , Issue.2 , pp. 627-635
    • Leduc, M.1    Frehel, C.2    Van Heijenoort, J.3
  • 57
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
    • Letain, T.E., and Postle, K. 1997. TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli. Mol. Microbiol. 24(2): 271-283. doi:10.1046/j.1365-2958.1997. 3331703.x. PMID:9159515. (Pubitemid 27223859)
    • (1997) Molecular Microbiology , vol.24 , Issue.2 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 58
    • 77949263042 scopus 로고    scopus 로고
    • A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation
    • doi:10.1038/nsmb.1770. PMID:20173761
    • Lewinson, O., Lee, A.T., Locher, K.P., and Rees, D.C. 2010. A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation. Nat. Struct. Mol. Biol. 17(3): 332-338. doi:10.1038/nsmb.1770. PMID:20173761.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , Issue.3 , pp. 332-338
    • Lewinson, O.1    Lee, A.T.2    Locher, K.P.3    Rees, D.C.4
  • 59
    • 0031025513 scopus 로고    scopus 로고
    • Molecular characterization of hpuAB, the haemoglobin-haptoglobin- utilization operon of Neisseria meningitidis
    • Lewis, L.A., Gray, E., Wang, Y.P., Roe, B.A., and Dyer, D.W. 1997. Molecular characterization of hpuAB, the haemoglobinhaptoglobin-utilization operon of Neisseria meningitidis. Mol. Microbiol. 23(4): 737-749. doi:10.1046/j.1365-2958.1997. 2501619.x. PMID:9157245. (Pubitemid 27072935)
    • (1997) Molecular Microbiology , vol.23 , Issue.4 , pp. 737-749
    • Lewis, L.A.1    Gray, E.2    Wang, Y.-P.3    Roe, B.A.4    Dyer, D.W.5
  • 60
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • DOI 10.1110/ps.0201402
    • Liu, Y., and Eisenberg, D. 2002. 3D domain swapping: as domains continue to swap. Protein Sci. 11(6): 1285-1299. doi:10.1110/ps. 0201402. PMID:12021428. (Pubitemid 34547201)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 61
    • 59849094863 scopus 로고    scopus 로고
    • Molecular characterization of the TonB2 protein from the fish pathogen Vibrio anguillarum
    • doi:10.1042/BJ20081462. PMID:18973471
    • Lopez, C.S., Peacock, R.S., Crosa, J.H., and Vogel, H.J. 2009. Molecular characterization of the TonB2 protein from the fish pathogen Vibrio anguillarum. Biochem. J. 418(1): 49-59.doi:10.1042/BJ20081462. PMID:18973471.
    • (2009) Biochem. J. , vol.418 , Issue.1 , pp. 49-59
    • Lopez, C.S.1    Peacock, R.S.2    Crosa, J.H.3    Vogel, H.J.4
  • 62
    • 0141994975 scopus 로고    scopus 로고
    • Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa
    • DOI 10.1128/JB.185.20.6112-6118.2003
    • Matias, V.R., Al-Amoudi, A., Dubochet, J., and Beveridge, T.J. 2003. Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa.J. Bacteriol. 185(20): 6112-6118. doi:10.1128/JB.185.20.61126118.2003. PMID:14526023. (Pubitemid 37248464)
    • (2003) Journal of Bacteriology , vol.185 , Issue.20 , pp. 6112-6118
    • Matias, V.R.F.1    Al-Amoudi, A.2    Dubochet, J.3    Beveridge, T.J.4
  • 63
    • 0025049224 scopus 로고
    • Import-defective colicin B derivatives mutated in the TonB box
    • doi:10.1111/j.1365-2958.1990.tb02063.x. PMID:2287276
    • Mende, J., and Braun, V. 1990. Import-defective colicin B derivatives mutated in the TonB box. Mol. Microbiol. 4(9): 1523-1533. doi:10.1111/j.1365- 2958.1990.tb02063.x. PMID:2287276.
    • (1990) Mol. Microbiol. , vol.4 , Issue.9 , pp. 1523-1533
    • Mende, J.1    Braun, V.2
  • 64
    • 77749233750 scopus 로고    scopus 로고
    • TonB-dependent transporters and their occurrence in cyanobacteria
    • doi:10.1186/17417007-7-68. PMID:19821963
    • Mirus, O., Strauss, S., Nicolaisen, K., von Haeseler, A., and Schleiff, E. 2009. TonB-dependent transporters and their occurrence in cyanobacteria. BMC Biol. 7(1): 68. doi:10.1186/17417007-7-68. PMID:19821963.
    • (2009) BMC Biol. , vol.7 , Issue.1 , pp. 68
    • Mirus, O.1    Strauss, S.2    Nicolaisen, K.3    Von Haeseler, A.4    Schleiff, E.5
  • 65
    • 16844366149 scopus 로고    scopus 로고
    • Import of the transfer RNase colicin D requires site-specific interaction with the energy-transducing protein TonB
    • DOI 10.1128/JB.187.8.2693-2697.2005
    • Mora, L., Diaz, N., Buckingham, R.H., and de Zamaroczy, M. 2005. Import of the transfer RNase colicin D requires site-specific interaction with the energy-transducing protein TonB. J. Bacteriol. 187(8): 2693-2697. doi:10.1128/JB.187.8.2693-2697.2005. PMID:15805515. (Pubitemid 40490373)
    • (2005) Journal of Bacteriology , vol.187 , Issue.8 , pp. 2693-2697
    • Mora, L.1    Diaz, N.2    Buckingham, R.H.3    De Zamaroczy, M.4
  • 66
    • 28844503096 scopus 로고    scopus 로고
    • ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus
    • DOI 10.1128/JB.187.24.8300-8311.2005
    • Neugebauer, H., Herrmann, C., Kammer, W., Schwarz, G., Nordheim, A., and Braun, V. 2005. ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus. J. Bacteriol. 187(24): 8300-8311. doi:10.1128/JB.187.24.8300-8311.2005. PMID:16321934. (Pubitemid 41780494)
    • (2005) Journal of Bacteriology , vol.187 , Issue.24 , pp. 8300-8311
    • Neugebauer, H.1    Herrmann, C.2    Kammer, W.3    Schwarz, G.4    Nordheim, A.5    Braun, V.6
  • 67
    • 0347479229 scopus 로고    scopus 로고
    • Molecular Basis of Bacterial Outer Membrane Permeability Revisited
    • DOI 10.1128/MMBR.67.4.593-656.2003
    • Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67(4): 593-656. doi:10.1128/MMBR.67.4.593-656.2003. PMID:14665678. (Pubitemid 37549772)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.4 , pp. 593-656
    • Nikaido, H.1
  • 68
    • 0037337264 scopus 로고    scopus 로고
    • Interactions between the outer membrane ferric citrate transporter FecA and TonB: Studies of the FecA TonB box
    • DOI 10.1128/JB.185.6.1870-1885.2003
    • Ogierman, M., and Braun, V. 2003. Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box. J. Bacteriol. 185(6): 1870-1885. doi:10. 1128/JB.185.6.1870-1885.2003. PMID:12618451. (Pubitemid 36297887)
    • (2003) Journal of Bacteriology , vol.185 , Issue.6 , pp. 1870-1885
    • Ogierman, M.1    Braun, V.2
  • 69
    • 33744791187 scopus 로고    scopus 로고
    • Structure of TonB in complex with FhuA, E. coli outer membrane receptor
    • DOI 10.1126/science.1128057
    • Pawelek, P.D., Croteau, N., Ng-Thow-Hing, C., Khursigara, C.M., Moiseeva, N., Allaire, M., and Coulton, J.W. 2006. Structure of TonB in complex with FhuA, E. coli outer membrane receptor. Science, 312(5778): 1399-1402. doi:10.1126/science.1128057. PMID:16741125. (Pubitemid 43839555)
    • (2006) Science , vol.312 , Issue.5778 , pp. 1399-1402
    • Pawelek, P.D.1    Croteau, N.2    Ng-Thow-Hing, C.3    Khursigara, C.M.4    Moiseeva, N.5    Allaire, M.6    Coulton, J.W.7
  • 71
    • 11844269327 scopus 로고    scopus 로고
    • The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides
    • DOI 10.1016/j.jmb.2004.11.026, PII S0022283604014652
    • Peacock, R.S., Weljie, A.M., Peter Howard, S., Price, F.D., and Vogel, H.J. 2005. The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides. J. Mol. Biol. 345(5): 1185-1197. doi:10.1016/j.jmb.2004.11. 026. PMID:15644214. (Pubitemid 40092233)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.5 , pp. 1185-1197
    • Sean Peacock, R.1    Weljie, A.M.2    Peter Howard, S.3    Price, F.D.4    Vogel, H.J.5
  • 73
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • DOI 10.1046/j.1365-2958.2003.03629.x
    • Postle, K., and Kadner, R.J. 2003. Touch and go: tying TonB to transport. Mol. Microbiol. 49(4): 869-882. doi:10.1046/j.1365-2958.2003.03629.x. PMID:12890014. (Pubitemid 36981335)
    • (2003) Molecular Microbiology , vol.49 , Issue.4 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 75
    • 0025992835 scopus 로고
    • Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
    • PMID:1885532
    • Roof, S.K., Allard, J.D., Bertrand, K.P., and Postle, K. 1991. Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions. J. Bacteriol. 173(17): 5554-5557. PMID:1885532.
    • (1991) J. Bacteriol. , vol.173 , Issue.17 , pp. 5554-5557
    • Roof, S.K.1    Allard, J.D.2    Bertrand, K.P.3    Postle, K.4
  • 76
    • 48749111115 scopus 로고    scopus 로고
    • Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: Implications for peptidoglycan recognition
    • doi:10.1073/pnas. 0803039105. PMID:18647830
    • Roujeinikova, A. 2008. Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: implications for peptidoglycan recognition. Proc. Natl. Acad. Sci. U.S.A. 105(30): 10348-10353. doi:10.1073/pnas. 0803039105. PMID:18647830.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.30 , pp. 10348-10353
    • Roujeinikova, A.1
  • 77
    • 0037337270 scopus 로고    scopus 로고
    • The unfolding story of three-dimensional domain swapping
    • DOI 10.1016/S0969-2126(03)00029-7, PII S0969212603000297
    • Rousseau, F., Schymkowitz, J.W., and Itzhaki, L.S. 2003. The unfolding story of three-dimensional domain swapping. Structure, 11(3): 243-251. doi:10.1016/S0969-2126(03)00029-7. PMID:12623012. (Pubitemid 36287689)
    • (2003) Structure , vol.11 , Issue.3 , pp. 243-251
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Itzhaki, L.S.3
  • 78
    • 0025271609 scopus 로고
    • Sequence of the fhuE outer-membrane receptor gene of Escherichia coli K12 and properties of mutants
    • doi:10. 1111/j.1365-2958.1990.tb00609.x. PMID:2162465
    • Sauer, M., Hantke, K., and Braun, V. 1990. Sequence of the fhuE outer-membrane receptor gene of Escherichia coli K12 and properties of mutants. Mol. Microbiol. 4(3): 427-437. doi:10. 1111/j.1365-2958.1990.tb00609.x. PMID:2162465.
    • (1990) Mol. Microbiol. , vol.4 , Issue.3 , pp. 427-437
    • Sauer, M.1    Hantke, K.2    Braun, V.3
  • 79
    • 0141727626 scopus 로고    scopus 로고
    • In vivo evidence for TonB dimerization
    • DOI 10.1128/JB.185.19.5747-5754.2003
    • Sauter, A., Howard, S.P., and Braun, V. 2003. In vivo evidence for TonB dimerization. J. Bacteriol. 185(19): 5747-5754. doi:10. 1128/JB.185.19.5747- 5754.2003. PMID:13129945. (Pubitemid 37176486)
    • (2003) Journal of Bacteriology , vol.185 , Issue.19 , pp. 5747-5754
    • Sauter, A.1    Howard, S.P.2    Braun, V.3
  • 80
    • 33846627273 scopus 로고    scopus 로고
    • Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery
    • DOI 10.1111/j.1365-2958.2006.05578.x
    • Schauer, K., Gouget, B., Carriere, M., Labigne, A., and de Reuse, H. 2007. Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery. Mol. Microbiol. 63(4): 1054-1068. doi:10.1111/j.1365-2958. 2006.05578.x. PMID:17238922. (Pubitemid 46184513)
    • (2007) Molecular Microbiology , vol.63 , Issue.4 , pp. 1054-1068
    • Schauer, K.1    Gouget, B.2    Carriere, M.3    Labigne, A.4    De Reuse, H.5
  • 81
    • 0024676062 scopus 로고
    • Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane
    • doi:10.1007/BF02464907. PMID:2549378
    • Schoffler, H., and Braun, V. 1989. Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane. Mol. Gen. Genet. 217(2-3): 378-383. doi:10.1007/BF02464907. PMID:2549378.
    • (1989) Mol. Gen. Genet. , vol.217 , Issue.2-3 , pp. 378-383
    • Schoffler, H.1    Braun, V.2
  • 82
    • 0023867105 scopus 로고
    • Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane
    • Sen, K., Hellman, J., and Nikaido, H. 1988. Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane. J. Biol. Chem. 263(3): 1182-1187. PMID:2447086. (Pubitemid 18039918)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.3 , pp. 1182-1187
    • Sen, K.1    Hellman, J.2    Nikaido, H.3
  • 83
    • 69949105383 scopus 로고    scopus 로고
    • Role of TonB1 in pyoverdinemediated signaling in Pseudomonas aeruginosa
    • doi:10.1128/JB.00742-09. PMID:19592589
    • Shirley, M., and Lamont, I.L. 2009. Role of TonB1 in pyoverdinemediated signaling in Pseudomonas aeruginosa. J. Bacteriol. 191(18): 5634-5640. doi:10.1128/JB.00742-09. PMID:19592589.
    • (2009) J. Bacteriol. , vol.191 , Issue.18 , pp. 5634-5640
    • Shirley, M.1    Lamont, I.L.2
  • 84
    • 33751557937 scopus 로고    scopus 로고
    • Neuroscience: The brain's dark energy
    • DOI 10.1126/science.
    • Shultis, D.D., Purdy, M.D., Banchs, C.N., and Wiener, M.C. 2006. uter membrane active transport: structure of the BtuB:TonB complex. Science, 312(5778): 1396-1399. doi:10.1126/science. 1127694. PMID:16741124. (Pubitemid 44846385)
    • (2006) Science , vol.314 , Issue.5803 , pp. 1249-1250
    • Raichle, M.E.1
  • 85
    • 77955283220 scopus 로고    scopus 로고
    • The bacterial cell envelope
    • doi:10.1101/cshperspect.a000414. PMID:20452953
    • Silhavy, T.J., Kahne, D., and Walker, S. 2010. The bacterial cell envelope. Cold Spring Harb. Perspect. Biol. 2(5): a000414. doi:10.1101/ cshperspect.a000414. PMID:20452953.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2 , Issue.5
    • Silhavy, T.J.1    Kahne, D.2    Walker, S.3
  • 87
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • DOI 10.1016/S1097-2765(01)00396-3
    • Soelaiman, S., Jakes, K., Wu, N., Li, C., and Shoham, M. 2001. Crystal structure of colicin E3: implications for cell entry and ribosome inactivation. Mol. Cell, 8(5): 1053-1062. doi:10.1016/S1097-2765(01)00396-3. PMID:11741540. (Pubitemid 34031807)
    • (2001) Molecular Cell , vol.8 , Issue.5 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.4    Shoham, M.5
  • 88
    • 0017703597 scopus 로고
    • Periplasmic space in Salmonella typhimurium and Escherichia coli
    • Stock, J.B., Rauch, B., and Roseman, S. 1977. Periplasmic space in Salmonella typhimurium and Escherichia coli. J. Biol. Chem. 252(21): 7850-7861. PMID:334768. (Pubitemid 8211043)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.21 , pp. 7850-7861
    • Stock, J.B.1    Rauch, B.2    Roseman, S.3
  • 89
    • 0028968322 scopus 로고
    • The Neisseria meningitidis haemoglobin receptor: Its role in iron utilization and virulence
    • doi:10.1111/j.1365-2958.1995.tb02266.x. PMID:7783623
    • Stojijkovic, I., Hwa, V., de Saint Martin, L., O'Gaora, P., Nassif, X., Heffron, F., and So, M. 1995. The Neisseria meningitidis haemoglobin receptor: its role in iron utilization and virulence. Mol. Microbiol. 15(3): 531-541. doi:10.1111/j.1365-2958.1995.tb02266.x. PMID:7783623.
    • (1995) Mol. Microbiol. , vol.15 , Issue.3 , pp. 531-541
    • Stojijkovic, I.1    Hwa, V.2    De Saint Martin, L.3    O'Gaora, P.4    Nassif, X.5    Heffron, F.6    So, M.7
  • 90
    • 33947364406 scopus 로고    scopus 로고
    • A novel protein, TtpC, is a required component of the TonB2 complex for specific iron transport in the pathogens Vibrio anguillarum and Vibrio cholerae
    • DOI 10.1128/JB.00451-06
    • Stork, M., Otto, B.R., and Crosa, J.H. 2007. A novel protein, TtpC, is a required component of the TonB2 complex for specific iron transport in the pathogens Vibrio anguillarum and Vibrio cholerae. J. Bacteriol. 189(5): 1803-1815. doi:10.1128/JB.0045106. PMID:17189363. (Pubitemid 46446143)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1803-1815
    • Stork, M.1    Otto, B.R.2    Crosa, J.H.3
  • 91
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer
    • Tieleman, D.P., and Berendsen, H.J. 1998. A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer. Bio-phys. J. 74(6): 2786-2801. doi:10.1016/S0006-3495(98)77986X. PMID:9635733. (Pubitemid 28268103)
    • (1998) Biophysical Journal , vol.74 , Issue.6 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 92
    • 0036778139 scopus 로고    scopus 로고
    • FepA with globular domain deletions lacks activity
    • DOI 10.1128/JB.184.19.5508-5512.2002
    • Vakharia, H.L., and Postle, K. 2002. FepA with globular domain deletions lacks activity. J. Bacteriol. 184(19): 5508-5512. doi:10.1128/JB.184.19.5508- 5512.2002. PMID:12218040. (Pubitemid 35024399)
    • (2002) Journal of Bacteriology , vol.184 , Issue.19 , pp. 5508-5512
    • Vakharia, H.L.1    Postle, K.2
  • 93
    • 0032528046 scopus 로고    scopus 로고
    • Crystal structure of a colicin N fragment suggests a model for toxicity
    • Vetter, I.R., Parker, M.W., Tucker, A.D., Lakey, J.H., Pattus, F., and Tsernoglou, D. 1998. Crystal structure of a colicin N fragment suggests a model for toxicity. Structure, 6(7): 863-874. doi:10.1016/S0969-2126(98)00088-4. PMID:9687368. (Pubitemid 28348649)
    • (1998) Structure , vol.6 , Issue.7 , pp. 863-874
    • Vetter, I.R.1    Parker, M.W.2    Tucker, A.D.3    Lakey, J.H.4    Pattus, F.5    Tsernoglou, D.6
  • 94
    • 75349104798 scopus 로고    scopus 로고
    • Architecture of peptidoglycan: More data and more models
    • doi:10.1016/j.tim.2009.12.004. PMID:20060721
    • Vollmer, W., and Seligman, S.J. 2010. Architecture of peptidoglycan: more data and more models. Trends Microbiol. 18(2): 59-66. doi:10.1016/j.tim.2009. 12.004. PMID:20060721.
    • (2010) Trends Microbiol. , vol.18 , Issue.2 , pp. 59-66
    • Vollmer, W.1    Seligman, S.J.2
  • 95
    • 0031022750 scopus 로고    scopus 로고
    • Crystal structure of colicin Ia
    • DOI 10.1038/385461a0
    • Wiener, M., Freymann, D., Ghosh, P., and Stroud, R.M. 1997. Crystal structure of colicin Ia. Nature, 385(6615): 461-464. doi:10.1038/385461a0. PMID:9009197. (Pubitemid 27065935)
    • (1997) Nature , vol.385 , Issue.6615 , pp. 461-464
    • Wiener, M.1    Freymann, D.2    Ghosh, P.3    Stroud, R.M.4
  • 96
    • 0042508859 scopus 로고    scopus 로고
    • Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA
    • DOI 10.1016/S0022-2836(03)00855-6
    • Yue, W.W., Grizot, S., and Buchanan, S.K. 2003. Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA. J. Mol. Biol. 332(2): 353-368. doi:10.1016/S0022- 2836(03)00855-6. PMID:12948487. (Pubitemid 37013505)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.2 , pp. 353-368
    • Yue, W.W.1    Grizot, S.2    Buchanan, S.K.3
  • 97
    • 54449087613 scopus 로고    scopus 로고
    • Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli
    • doi:10.1074/jbc.M802591200. PMID:18640984
    • Zeth, K., Romer, C., Patzer, S.I., and Braun, V. 2008. Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli. J. Biol. Chem. 283(37): 25324-25331. doi:10.1074/jbc.M802591200. PMID:18640984.
    • (2008) J. Biol. Chem. , vol.283 , Issue.37 , pp. 25324-25331
    • Zeth, K.1    Romer, C.2    Patzer, S.I.3    Braun, V.4
  • 98
    • 75149149839 scopus 로고    scopus 로고
    • The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins
    • doi:10.1111/j.1365-2958.2009.06808.x. PMID:19627502
    • Zhang, Y., Li, C., Vankemmelbeke, M.N., Bardelang, P., Paoli, M., Penfold, C.N., and James, R. 2010. The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins. Mol. Microbiol. 75(3): 623-636. doi:10.1111/j.1365-2958.2009.06808.x. PMID:19627502.
    • (2010) Mol. Microbiol. , vol.75 , Issue.3 , pp. 623-636
    • Zhang, Y.1    Li, C.2    Vankemmelbeke, M.N.3    Bardelang, P.4    Paoli, M.5    Penfold, C.N.6    James, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.