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Volumn 9, Issue , 2011, Pages

Engineering of an E. coli outer membrane protein FhuA with increased channel diameter

Author keywords

Channel proteins; FhuA; HRP; Liposomes; Nanocontainers; Protein engineering; TMB Assay

Indexed keywords

CHANNEL PROTEINS; FHUA; HRP; NANOCONTAINERS; PROTEIN ENGINEERING; TMB-ASSAY;

EID: 80051786355     PISSN: None     EISSN: 14773155     Source Type: Journal    
DOI: 10.1186/1477-3155-9-33     Document Type: Article
Times cited : (25)

References (36)
  • 1
    • 0030220261 scopus 로고    scopus 로고
    • Porins: general to specific, native to engineered passive pores
    • 10.1016/S0959-440X(96)80113-8, 8794162
    • Schulz G. Porins: general to specific, native to engineered passive pores. Curr Opin Struct Biol 1996, 6:485-490. 10.1016/S0959-440X(96)80113-8, 8794162.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 485-490
    • Schulz, G.1
  • 2
    • 0036441481 scopus 로고    scopus 로고
    • Secondary and tertiary structure formation of the b-barrel membrane protein OmpA is synchronized and depends on membrane thickness
    • 10.1016/S0022-2836(02)01071-9, 12441110
    • Kleinschmidt JH, KT T. Secondary and tertiary structure formation of the b-barrel membrane protein OmpA is synchronized and depends on membrane thickness. J Mol Biol 2002, 324:319-330. 10.1016/S0022-2836(02)01071-9, 12441110.
    • (2002) J Mol Biol , vol.324 , pp. 319-330
    • Kleinschmidt, J.H.1    KT, T.2
  • 3
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • Ramachandran R, Heuck AP, Tweten RK, Johnson AE. Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nat Struct Biol 2002, 9:823-827.
    • (2002) Nat Struct Biol , vol.9 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 4
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • Wimley C. The versatile beta-barrel membrane protein. Curr Opin Struc Biol 2003, 13:404-411.
    • (2003) Curr Opin Struc Biol , vol.13 , pp. 404-411
    • Wimley, C.1
  • 5
    • 4444258925 scopus 로고    scopus 로고
    • Crystal structure of the bacterial nucleoside transporter Tsx
    • 10.1038/sj.emboj.7600330, 514505, 15272310
    • Ye J, van den Berg B. Crystal structure of the bacterial nucleoside transporter Tsx. EMBO J 2004, 23:3187-3195. 10.1038/sj.emboj.7600330, 514505, 15272310.
    • (2004) EMBO J , vol.23 , pp. 3187-3195
    • Ye, J.1    van den Berg, B.2
  • 7
    • 33646064116 scopus 로고    scopus 로고
    • A nanocompartment system (synthosome) designed for biotechnological applications
    • 10.1016/j.jbiotec.2005.10.025, 16364484
    • Nallani M, Benito S, Onaca O, Graff A, Lindemann M, Winterhalter M, Meier W, Schwaneberg U. A nanocompartment system (synthosome) designed for biotechnological applications. J Biotechnol 2006, 123:50-59. 10.1016/j.jbiotec.2005.10.025, 16364484.
    • (2006) J Biotechnol , vol.123 , pp. 50-59
    • Nallani, M.1    Benito, S.2    Onaca, O.3    Graff, A.4    Lindemann, M.5    Winterhalter, M.6    Meier, W.7    Schwaneberg, U.8
  • 8
    • 28144463963 scopus 로고    scopus 로고
    • Therapeutic nanoreactors: combining chemistry and biology in a novel triblock copolymer drug delivery system
    • 10.1021/nl051523d, 16277457
    • Ranquin A, Versees W, Meier W, Steyaert J, Van Gelder P. Therapeutic nanoreactors: combining chemistry and biology in a novel triblock copolymer drug delivery system. Nano Lett 2005, 5:2220-2224. 10.1021/nl051523d, 16277457.
    • (2005) Nano Lett , vol.5 , pp. 2220-2224
    • Ranquin, A.1    Versees, W.2    Meier, W.3    Steyaert, J.4    Van Gelder, P.5
  • 9
    • 0030045746 scopus 로고    scopus 로고
    • Folding and membrane insertion of the trimeric beta-barrel protein OmpF
    • 10.1021/bi951216u, 8652568
    • Surrey T, Schmid A, Jähnig F. Folding and membrane insertion of the trimeric beta-barrel protein OmpF. Biochemistry 1996, 35:2283-2288. 10.1021/bi951216u, 8652568.
    • (1996) Biochemistry , vol.35 , pp. 2283-2288
    • Surrey, T.1    Schmid, A.2    Jähnig, F.3
  • 10
    • 0022500907 scopus 로고
    • Overproduction of the proFhuA outer membrane receptor protein of Escherichia coli K-12: isolation, properties, and immunocytochemical localization at the inner side of the cytoplasmic membrane
    • 10.1007/BF00470867, 3539058
    • Hoffmann H, Fischer E, Schwarz H, Braun V. Overproduction of the proFhuA outer membrane receptor protein of Escherichia coli K-12: isolation, properties, and immunocytochemical localization at the inner side of the cytoplasmic membrane. Arch Microbiol 1986, 145:334-341. 10.1007/BF00470867, 3539058.
    • (1986) Arch Microbiol , vol.145 , pp. 334-341
    • Hoffmann, H.1    Fischer, E.2    Schwarz, H.3    Braun, V.4
  • 11
    • 0034079929 scopus 로고    scopus 로고
    • Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA
    • Ferguson A, Braun V, Fiedler H-P, Coulton J, Diederichs K, Welte W. Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Prot Sci 2000, 9:956-963.
    • (2000) Prot Sci , vol.9 , pp. 956-963
    • Ferguson, A.1    Braun, V.2    Fiedler, H.-P.3    Coulton, J.4    Diederichs, K.5    Welte, W.6
  • 12
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: crystal structure bound lipopolysaccharide
    • Ferguson A, Hofmann E, Coulton J, Diederichs K. Siderophore-mediated iron transport: crystal structure bound lipopolysaccharide. Science 1998, 282:2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.1    Hofmann, E.2    Coulton, J.3    Diederichs, K.4
  • 13
    • 0036411842 scopus 로고    scopus 로고
    • Diffusion through channel derivatives of the Escherichia coli FhuA transport protein
    • 10.1046/j.1432-1033.2002.03195.x, 12383253
    • Braun M, Killmann H, Maier E, Benz R, Braun V. Diffusion through channel derivatives of the Escherichia coli FhuA transport protein. Eur J Biochem 2002, 269:4948-4959. 10.1046/j.1432-1033.2002.03195.x, 12383253.
    • (2002) Eur J Biochem , vol.269 , pp. 4948-4959
    • Braun, M.1    Killmann, H.2    Maier, E.3    Benz, R.4    Braun, V.5
  • 15
    • 77955103129 scopus 로고    scopus 로고
    • Molecular understanding of sterically controlled compound release through an engineered channel protein (FhuA)
    • Güven A, Fioroni M, Hauer B, Schwaneberg U. Molecular understanding of sterically controlled compound release through an engineered channel protein (FhuA). J Nanobiotech 2010, 8(14).
    • (2010) J Nanobiotech , vol.8 , Issue.14
    • Güven, A.1    Fioroni, M.2    Hauer, B.3    Schwaneberg, U.4
  • 16
    • 79952693498 scopus 로고    scopus 로고
    • Engineering of the E. coli Outer Membrane Protein FhuA to overcome the Hydrophobic Mismatch in Thick Polymeric Membranes
    • Muhammad N, Dworeck T, Fioroni M, Schwaneberg U. Engineering of the E. coli Outer Membrane Protein FhuA to overcome the Hydrophobic Mismatch in Thick Polymeric Membranes. J Nanobiotech 2011, 9(8).
    • (2011) J Nanobiotech , vol.9 , Issue.8
    • Muhammad, N.1    Dworeck, T.2    Fioroni, M.3    Schwaneberg, U.4
  • 17
    • 0034659796 scopus 로고    scopus 로고
    • Rigid-rod beta-barrels as lipocalin models: probing confined space by carotenoid encapsulation
    • Baumeister B, Matile S. Rigid-rod beta-barrels as lipocalin models: probing confined space by carotenoid encapsulation. Chem - Eur J 2000, 6:1739-1749.
    • (2000) Chem - Eur J , vol.6 , pp. 1739-1749
    • Baumeister, B.1    Matile, S.2
  • 18
    • 0142062495 scopus 로고    scopus 로고
    • Synthetic multifunctional pores: lessons from rigid-rod beta-barrels
    • Sakai N, Matile S. Synthetic multifunctional pores: lessons from rigid-rod beta-barrels. Chem Commun 2003, 2514-2523.
    • (2003) Chem Commun , pp. 2514-2523
    • Sakai, N.1    Matile, S.2
  • 19
    • 0347359146 scopus 로고    scopus 로고
    • Molecular rods. 1. Simple axial rods
    • 10.1021/cr970070x, 11849014
    • Schwab PFH, Levin MD, Michl J. Molecular rods. 1. Simple axial rods. Chem Rev 1999, 99:1863-1934. 10.1021/cr970070x, 11849014.
    • (1999) Chem Rev , vol.99 , pp. 1863-1934
    • Schwab, P.F.H.1    Levin, M.D.2    Michl, J.3
  • 20
    • 4043107662 scopus 로고    scopus 로고
    • Thermodynamic and kinetic stability of synthetic multifunctional rigid-rod β-barrel pores: evidence for supramolecular catalysis
    • 10.1021/ja0481878, 15303883
    • Litvinchuk S, Bollot G, Mareda J, Som A, Ronan D, Shah MR, Perrottet P, Sakai N, Matile S. Thermodynamic and kinetic stability of synthetic multifunctional rigid-rod β-barrel pores: evidence for supramolecular catalysis. J Am Chem Soc 2004, 126:10067-10075. 10.1021/ja0481878, 15303883.
    • (2004) J Am Chem Soc , vol.126 , pp. 10067-10075
    • Litvinchuk, S.1    Bollot, G.2    Mareda, J.3    Som, A.4    Ronan, D.5    Shah, M.R.6    Perrottet, P.7    Sakai, N.8    Matile, S.9
  • 21
    • 25844530053 scopus 로고    scopus 로고
    • AFM snapshots of synthetic multifunctional pores with polyacetylene blockers: Pseudorotaxanes and template effects
    • Kumaki J, Yashima E, Bollot G, Mareda J, Litvinchuk S, Matile S. AFM snapshots of synthetic multifunctional pores with polyacetylene blockers: Pseudorotaxanes and template effects. Angew Chem, Int Ed 2005, 44:6154-6157.
    • (2005) Angew Chem, Int Ed , vol.44 , pp. 6154-6157
    • Kumaki, J.1    Yashima, E.2    Bollot, G.3    Mareda, J.4    Litvinchuk, S.5    Matile, S.6
  • 22
    • 12744280086 scopus 로고    scopus 로고
    • Blockage of rigid-rod beta-barrel pores by rigid-rod R-helix mimics
    • Litvinchuk S, Matile S. Blockage of rigid-rod beta-barrel pores by rigid-rod R-helix mimics. Supramol Chem 2005, 17:135-139.
    • (2005) Supramol Chem , vol.17 , pp. 135-139
    • Litvinchuk, S.1    Matile, S.2
  • 24
    • 79951960730 scopus 로고    scopus 로고
    • FhuA Deletion Variant del1-159 Overexpression in Inclusion Bodies and Refolding with Polyethylene-Poly(ethylene glycol) Diblock Copolymer
    • Dworeck T, Petri AK, Muhammad N, Fioroni M, Schwaneberg U. FhuA Deletion Variant del1-159 Overexpression in Inclusion Bodies and Refolding with Polyethylene-Poly(ethylene glycol) Diblock Copolymer. Prot Expr Purif 2011, 77(1):75-79.
    • (2011) Prot Expr Purif , vol.77 , Issue.1 , pp. 75-79
    • Dworeck, T.1    Petri, A.K.2    Muhammad, N.3    Fioroni, M.4    Schwaneberg, U.5
  • 25
    • 0010287406 scopus 로고    scopus 로고
    • Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane
    • 10.1021/bi9608673, 8916906
    • Boulanger P, le Marie M, Bonhivers M, Dubois S, Desmadril S, Letellier L. Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane. Biochemistry 1996, 35:14216-14224. 10.1021/bi9608673, 8916906.
    • (1996) Biochemistry , vol.35 , pp. 14216-14224
    • Boulanger, P.1    le Marie, M.2    Bonhivers, M.3    Dubois, S.4    Desmadril, S.5    Letellier, L.6
  • 26
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • Andrade M, Chacón P, Merelo J, Morán F. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Prot Eng 1993, 6:383-390.
    • (1993) Prot Eng , vol.6 , pp. 383-390
    • Andrade, M.1    Chacón, P.2    Merelo, J.3    Morán, F.4
  • 27
    • 0020478887 scopus 로고
    • The horseradish peroxidase-catalyzed oxidation of 3,5,3',5'-tetramethylbenzidine. Free radical and chargetransfer complex intermediates
    • Josephy P, Eling T, Mason R. The horseradish peroxidase-catalyzed oxidation of 3,5,3',5'-tetramethylbenzidine. Free radical and chargetransfer complex intermediates. J of Biol Chem 1982, 257:3669-3675.
    • (1982) J of Biol Chem , vol.257 , pp. 3669-3675
    • Josephy, P.1    Eling, T.2    Mason, R.3
  • 28
    • 0020478887 scopus 로고
    • The horseradish peroxidase-catalyzed oxidation of 3,5,3',5'-tetramethylbenzidine. Free radical and charge-transfer complex intermediates
    • Josephy P, Eling T, Mason R. The horseradish peroxidase-catalyzed oxidation of 3,5,3',5'-tetramethylbenzidine. Free radical and charge-transfer complex intermediates. J Biol Chem 1982, 257:3669-3675.
    • (1982) J Biol Chem , vol.257 , pp. 3669-3675
    • Josephy, P.1    Eling, T.2    Mason, R.3
  • 29
    • 0031780180 scopus 로고    scopus 로고
    • Identification and characterization of two quiescent porin genes, nmpC and ompN, in Escherichia coli B
    • 107294, 9642192
    • Prilipov A, Phale P, Koebnik R, Widmer C, Rosenbusch J. Identification and characterization of two quiescent porin genes, nmpC and ompN, in Escherichia coli B. J Bacteriol 1998, 180:3388-3392. 107294, 9642192.
    • (1998) J Bacteriol , vol.180 , pp. 3388-3392
    • Prilipov, A.1    Phale, P.2    Koebnik, R.3    Widmer, C.4    Rosenbusch, J.5
  • 30
    • 0033954070 scopus 로고    scopus 로고
    • Effects of calcium and calcium chelators on growth and morphology of Escherichia coli L-form NC-7
    • 10.1128/JB.182.5.1419-1422.2000, 94432, 10671467
    • Onoda T, Enokizono J, Kaya H, Oshima A, Freestone P, Norris V. Effects of calcium and calcium chelators on growth and morphology of Escherichia coli L-form NC-7. J Bacteriol 2000, 182(5):1419-1422. 10.1128/JB.182.5.1419-1422.2000, 94432, 10671467.
    • (2000) J Bacteriol , vol.182 , Issue.5 , pp. 1419-1422
    • Onoda, T.1    Enokizono, J.2    Kaya, H.3    Oshima, A.4    Freestone, P.5    Norris, V.6
  • 31
    • 0030850807 scopus 로고    scopus 로고
    • Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes
    • 10.1111/j.1432-1033.1997.t01-1-00770.x, 9288896
    • Locher KP, Rosenbusch JP. Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes. Eur J Biochem 1997, 247(3):770-775. 10.1111/j.1432-1033.1997.t01-1-00770.x, 9288896.
    • (1997) Eur J Biochem , vol.247 , Issue.3 , pp. 770-775
    • Locher, K.P.1    Rosenbusch, J.P.2
  • 32
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • 10.1016/S0092-8674(00)81700-6, 9865695
    • Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbusch JP, Moras D. Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 1998, 95:771-778. 10.1016/S0092-8674(00)81700-6, 9865695.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0, 5432063
    • Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685. 10.1038/227680a0, 5432063.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 34
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structures content of proteins from circular dichroism spectrum
    • Deléage G, Geourjon C. An interactive graphic program for calculating the secondary structures content of proteins from circular dichroism spectrum. Comput Appl Biosci 1993, 2:197-199.
    • (1993) Comput Appl Biosci , vol.2 , pp. 197-199
    • Deléage, G.1    Geourjon, C.2
  • 35
    • 0020176542 scopus 로고
    • An eigenfunction expansion method for the analysis of exponential decay curves
    • Provencher SW. An eigenfunction expansion method for the analysis of exponential decay curves. Comput Phys Commun 1982, 27:213-227.
    • (1982) Comput Phys Commun , vol.27 , pp. 213-227
    • Provencher, S.W.1


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