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Volumn 1838, Issue 1 PARTB, 2014, Pages 364-371

FhuA interactions in a detergent-free nanodisc environment

Author keywords

Barrel proteins; Channels; Membrane; Nanodiscs; Siderophore; Transporters

Indexed keywords

COLICIN; DETERGENT; FERRIC HYDROXAMATE UPTAKE PROTEIN COMPONENT A; NANODISC; PROTEIN TONB; SIDEROPHORE;

EID: 84887933251     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.09.022     Document Type: Article
Times cited : (20)

References (37)
  • 1
    • 0030850807 scopus 로고    scopus 로고
    • Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes
    • K.P. Locher, and J.P. Rosenbusch Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes Eur. J. Biochem. 247 1997 770 775 (Pubitemid 27337027)
    • (1997) European Journal of Biochemistry , vol.247 , Issue.3 , pp. 770-775
    • Locher, K.P.1    Rosenbusch, J.P.2
  • 2
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • DOI 10.1126/science.282.5397.2215
    • A.D. Ferguson, E. Hofmann, J.W. Coulton, K. Diederichs, and W. Welte Siderophore-mediation iron transport: crystal structure of FhuA with bound lipopolysaccharides Science 282 1998 2215 2220 (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
  • 3
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • DOI 10.1016/S0092-8674(00)81700-6
    • K.P. Locher, B. Rees, R. Koebnik, A. Mitschler, L. Moulinier, J.P. Rosenbusch, and D. Moras Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferricrhome bound states reveal allosteric changes Cell 95 1998 771 778 (Pubitemid 29014457)
    • (1998) Cell , vol.95 , Issue.6 , 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
  • 4
    • 78651364685 scopus 로고    scopus 로고
    • TonB or not TonB: Is that the question?
    • K.D. Krewulak, and H.J. Vogel TonB or not TonB: is that the question? Biochem. Cell Biol. 89 2011 87 97
    • (2011) Biochem. Cell Biol. , vol.89 , pp. 87-97
    • Krewulak, K.D.1    Vogel, H.J.2
  • 5
    • 0015891744 scopus 로고
    • A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B
    • V. Braun, K. Schaller, and H. Wolf A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B Biochim. Biophys. Acta 323 1973 87 97
    • (1973) Biochim. Biophys. Acta , vol.323 , pp. 87-97
    • Braun, V.1    Schaller, K.2    Wolf, H.3
  • 8
    • 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
    • H. Schöffler, and V. Braun 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 1989 378 383
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 378-383
    • Schöffler, H.1    Braun, V.2
  • 9
    • 0043165150 scopus 로고    scopus 로고
    • Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity
    • DOI 10.1128/JB.185.16.4683-4692.2003
    • F. Endriß, M. Braun, H. Killmann, and V. Braun Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity J. Bacteriol. 185 2003 4683 4692 (Pubitemid 36962274)
    • (2003) Journal of Bacteriology , vol.185 , Issue.16 , pp. 4683-4692
    • Endriss, F.1    Braun, M.2    Killmann, H.3    Braun, V.4
  • 10
    • 14644388782 scopus 로고    scopus 로고
    • Kinetic analyses reveal multiple steps in forming TonB-FhuA complexes from Escherichia coli
    • DOI 10.1021/bi047882p
    • C.M. Khursigara, G. De Crescenzo, P.D. Pawelek, and J.W. Coulton Kinetic analyses reveal multiple steps in forming TonB-FhuA complexes from Escherichia coli Biochemistry 44 2005 3441 3453 (Pubitemid 40322014)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3441-3453
    • Khursigara, C.M.1    De Crescenzo, G.2    Pawelek, P.D.3    Coulton, J.W.4
  • 11
    • 33744780736 scopus 로고    scopus 로고
    • Outer membrane active transport: Structure of the BtuB:TonB complex
    • DOI 10.1126/science.1127694
    • D.D. Shultis, M.D. Purdy, C.N. Banchs, and M.C. Wiener Outer membrane active transport: structure of the BtuB:TonB complex Science 312 2006 1396 1399 (Pubitemid 43839554)
    • (2006) Science , vol.312 , Issue.5778 , pp. 1396-1399
    • Shultis, D.D.1    Purdy, M.D.2    Banchs, C.N.3    Wiener, M.C.4
  • 12
    • 33748657558 scopus 로고    scopus 로고
    • Interaction of TonB with the outer membrane receptor FpvA of Pseudomonas aeruginosa
    • DOI 10.1128/JB.00435-06
    • H. Adams, G. Zeder-Lutz, I. Schalk, F. Pattus, and H. Celia Interaction of TonB with the outer membrane receptor FpvA of Pseudomonas aeruginosa J. Bacteriol. 188 2006 5752 5761 (Pubitemid 44384083)
    • (2006) Journal of Bacteriology , vol.188 , Issue.16 , pp. 5752-5761
    • Adams, H.1    Zeder-Lutz, G.2    Schalk, I.3    Pattus, F.4    Celia, H.5
  • 13
    • 84876274460 scopus 로고    scopus 로고
    • Monomeric TonB and the TonB box are required for the formation of a high-affinity Transporter-TonB complex
    • D.M. Freed, S.M. Lukasik, A. Sikora, A. Mokdad, and D.S. Cafiso Monomeric TonB and the TonB box are required for the formation of a high-affinity Transporter-TonB complex Biochemistry 52 2013 2638 2648
    • (2013) Biochemistry , vol.52 , pp. 2638-2648
    • Freed, D.M.1    Lukasik, S.M.2    Sikora, A.3    Mokdad, A.4    Cafiso, D.S.5
  • 14
    • 34247214427 scopus 로고    scopus 로고
    • Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    • DOI 10.1038/sj.emboj.7601661, PII 7601661
    • M. Alami, K. Dalal, B. Lelj-Garolla, S.G. Sligar, and F. Duong Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA EMBO J. 26 2007 1995 2004 (Pubitemid 46625796)
    • (2007) EMBO Journal , vol.26 , Issue.8 , pp. 1995-2004
    • Alami, M.1    Dalal, K.2    Lelj-Garolla, B.3    Sligar, S.G.4    Duong, F.5
  • 16
    • 84873400562 scopus 로고    scopus 로고
    • Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins
    • F. Hagn, M. Etzkorn, T. Raschle, and G. Wagner Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins J. Am. Chem. Soc. 135 2012 1919 1925
    • (2012) J. Am. Chem. Soc. , vol.135 , pp. 1919-1925
    • Hagn, F.1    Etzkorn, M.2    Raschle, T.3    Wagner, G.4
  • 17
    • 71749095971 scopus 로고    scopus 로고
    • Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs
    • T. Raschle, S. Hiller, T.-Y. Yu, A.J. Rice, T. Walz, and G. Wagner Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs J. Am. Chem. Soc. 131 2009 17777 17779
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17777-17779
    • Raschle, T.1    Hiller, S.2    Yu, T.-Y.3    Rice, A.J.4    Walz, T.5    Wagner, G.6
  • 18
    • 0017254020 scopus 로고
    • Siderophore protection against colicins M, B, V, and Ia in Escherichia coli
    • R. Wayne, K. Frick, and J.B. Neilands Siderophore protection against colicins M, B, V, and Ia in Escherichia coli J. Bacteriol. 126 1 1976 7 12
    • (1976) J. Bacteriol. , vol.126 , Issue.1 , pp. 7-12
    • Wayne, R.1    Frick, K.2    Neilands, J.B.3
  • 19
    • 0029836552 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12
    • G.S. Moeck, P. Tawa, H. Xiang, A.A. Ismail, J.L. Turnbull, and J.W. Coulton Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12 Mol. Microbiol. 22 1996 459 471 (Pubitemid 26373831)
    • (1996) Molecular Microbiology , vol.22 , Issue.3 , pp. 459-471
    • Moeck, G.S.1    Tawa, P.2    Xiang, H.3    Ismail, A.A.4    Turnbull, J.L.5    Coulton, J.W.6
  • 20
    • 33747354636 scopus 로고    scopus 로고
    • Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors
    • M.E. Ghachi, A. Bouhss, H. Barreteau, T. Touzé, G. Auger, D. Blanot, and D. Mengin-Lecreulx Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors J. Biol. Chem. 281 2006 22761 22772
    • (2006) J. Biol. Chem. , vol.281 , pp. 22761-22772
    • Ghachi, M.E.1    Bouhss, A.2    Barreteau, H.3    Touzé, T.4    Auger, G.5    Blanot, D.6    Mengin-Lecreulx, D.7
  • 21
    • 1642382983 scopus 로고    scopus 로고
    • Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
    • DOI 10.1021/ja0393574
    • I.G. Denisov, Y.V. Grinkova, A.A. Lazarides, and S.G. Sligar Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size J. Am. Chem. Soc. 126 2004 3477 3487 (Pubitemid 38366738)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.11 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 22
    • 35448962899 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: Experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions
    • J.J. Correia, H.W. Detrich III Academic Press San Diego, CA
    • M.W. Freyer, and E.A. Lewis Isothermal titration calorimetry: experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions J.J. Correia, H.W. Detrich III Methods in Cell Biology vol. 84 2008 Academic Press San Diego, CA
    • (2008) Methods in Cell Biology , vol.84 VOL.
    • Freyer, M.W.1    Lewis, E.A.2
  • 23
    • 77954733211 scopus 로고    scopus 로고
    • Reconstitution of the SecY translocon in nanodiscs
    • K. Dalal, and F. Duong Reconstitution of the SecY translocon in nanodiscs Methods Mol. Biol. 619 2010 145 156
    • (2010) Methods Mol. Biol. , vol.619 , pp. 145-156
    • Dalal, K.1    Duong, F.2
  • 24
    • 0035045544 scopus 로고    scopus 로고
    • Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA
    • DOI 10.1128/JB.183.9.2755-2764.2001
    • G.S. Moeck, and L. Letellier Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA J. Bacteriol. 183 9 2001 2755 2764 (Pubitemid 32319277)
    • (2001) Journal of Bacteriology , vol.183 , Issue.9 , pp. 2755-2764
    • Moeck, G.S.1    Letellier, L.2
  • 25
    • 0028942302 scopus 로고
    • Identification of receptor binding sites by competitive peptide mapping: Phages T1, T5, and Φ80 and colicin M bind to the gating loop of FhuA
    • H. Killmann, G. Videnov, G. Jung, H. Schwarz, and V. Braun Identification of receptor binding sites by competitive peptide mapping: phages T1, T5, and Φ80 and colicin M bind to the gating loop of FhuA J. Bacteriol. 177 3 1995 694 698
    • (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
  • 26
    • 84870209727 scopus 로고    scopus 로고
    • Import of periplasmic bacteriocins targeting the murein
    • V. Braun, S. Helbig, and S.I. Patzer Import of periplasmic bacteriocins targeting the murein Biochem. Soc. Trans. 40 2012 1449 1455
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1449-1455
    • Braun, V.1    Helbig, S.2    Patzer, S.I.3
  • 28
    • 0029116515 scopus 로고
    • Mutual inhibition of cobalamin and siderophore uptake systems suggests their competition for TonB function
    • R.J. Kadner, and K.J. Heller Mutual inhibition of cobalamin and siderophore uptake systems suggests their competition for TonB function J. Bacteriol. 177 1995 4829 4835
    • (1995) J. Bacteriol. , vol.177 , pp. 4829-4835
    • Kadner, R.J.1    Heller, K.J.2
  • 29
    • 41549103706 scopus 로고    scopus 로고
    • Visualization of interactions between siderophore transporters and the energizing protein TonB by native PAGE
    • DOI 10.1002/elps.200700612
    • S. Choul-Li, H. Adams, F. Pattus, and H. Celia Visualization of interactions between siderophore transporters and the energizing protein TonB by native PAGE Electrophoresis 29 2008 1333 1338 (Pubitemid 351461087)
    • (2008) Electrophoresis , vol.29 , Issue.6 , pp. 1333-1338
    • Choul-Li, S.1    Adams, H.2    Pattus, F.3    Celia, H.4
  • 30
    • 0242415191 scopus 로고    scopus 로고
    • Membrane mimetic environments alter the conformation of the outer membrane protein BtuB
    • G.E. Fanucci, J.Y. Lee, and D.S. Cafiso Membrane mimetic environments alter the conformation of the outer membrane protein BtuB J. Am. Chem. Soc. 125 2003 12933 13932
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12933-13932
    • Fanucci, G.E.1    Lee, J.Y.2    Cafiso, D.S.3
  • 31
    • 1542320184 scopus 로고    scopus 로고
    • Enhanced Binding of TonB to a Ligand-loaded Outer Membrane Receptor: Role of the oligomeric state of TonB in formation of a functional FhuA·TonB complex
    • DOI 10.1074/jbc.M311784200
    • C.M. Khursigara, G. De Crescenzo, P.D. Pawelek, and J.W. Coulton Enhanced binding of TonB to a ligand-loaded outer membrane receptor: role of the oligomeric state of TonB in formation of a functional FhuA-TonB complex J. Biol. Chem. 279 2004 7405 7412 (Pubitemid 38294616)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7405-7412
    • Khursigara, C.M.1    De Crescenzo, G.2    Pawelek, P.D.3    Coulton, J.W.4
  • 32
    • 41949109350 scopus 로고    scopus 로고
    • Modulation by substrates of the interaction between the HasR outer membrane receptor and its specific TonB-like protein, HasB
    • J. Lefèvre, P. Delepelaire, M. Delepierre, and N. Izadi-Pruneyre Modulation by substrates of the interaction between the HasR outer membrane receptor and its specific TonB-like protein, HasB J. Mol. Biol. 378 2008 840 851
    • (2008) J. Mol. Biol. , vol.378 , pp. 840-851
    • Lefèvre, J.1    Delepelaire, P.2    Delepierre, M.3    Izadi-Pruneyre, N.4
  • 33
    • 35948949060 scopus 로고    scopus 로고
    • A β Strand Lock Exchange for Signal Transduction in TonB-Dependent Transducers on the Basis of a Common Structural Motif
    • DOI 10.1016/j.str.2007.08.013, PII S0969212607003401
    • K. Brillet, L. Journet, H. Célia, L. Paulus, A. Stahl, F. Pattus, and D. Cobessi A β-strand lock exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif Structure 15 2007 1383 1391 (Pubitemid 350064492)
    • (2007) Structure , vol.15 , Issue.11 , pp. 1383-1391
    • Brillet, K.1    Journet, L.2    Celia, H.3    Paulus, L.4    Stahl, A.5    Pattus, F.6    Cobessi, D.7
  • 35
    • 0015523816 scopus 로고
    • Interaction of colicin Ia with bacterial cells. Direct measurement of Ia-receptor interaction
    • J. Konisky, and B.S. Cowell Interaction of colicin Ia with bacterial cells. Direct measurement of Ia-receptor interaction J. Biol. Chem. 247 1972 6524 6529
    • (1972) J. Biol. Chem. , vol.247 , pp. 6524-6529
    • Konisky, J.1    Cowell, B.S.2
  • 36
    • 0019889063 scopus 로고
    • Thermodynamics of protein association interactions: Forces contributing to stability
    • P.D. Ross, and S. Subramanian Thermodynamics of protein association interactions: forces contributing to stability Biochemistry 20 1981 3096 3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 37
    • 79551485286 scopus 로고    scopus 로고
    • Mapping functional domains of colicin M
    • Helbig S.Braun V.Mapping functional domains of colicin M J. Bacteriol.2011 193 815-821
    • (2011) J. Bacteriol. , vol.193 , pp. 815-821
    • Helbig, S.1    Braun, V.2


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