메뉴 건너뛰기




Volumn 10, Issue 8, 2014, Pages

Structure of CfaA Suggests a New Family of Chaperones Essential for Assembly of Class 5 Fimbriae

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; CFAA PROTEIN; CHAPERONE; LYSINE; PILIN; UNCLASSIFIED DRUG; FIMBRIA PROTEIN;

EID: 84919402884     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004316     Document Type: Article
Times cited : (9)

References (46)
  • 1
    • 84858215567 scopus 로고    scopus 로고
    • Chaperone-usher pathways: diversity and pilus assembly mechanism
    • Busch A, Waksman G, (2012) Chaperone-usher pathways: diversity and pilus assembly mechanism. Philos Trans R Soc Lond B Biol Sci 367: 1112–1122.
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , pp. 1112-1122
    • Busch, A.1    Waksman, G.2
  • 2
    • 0024468229 scopus 로고
    • Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
    • Holmgren A, Branden CI, (1989) Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature 342: 248–251.
    • (1989) Nature , vol.342 , pp. 248-251
    • Holmgren, A.1    Branden, C.I.2
  • 3
    • 0033551911 scopus 로고    scopus 로고
    • X-ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Escherichia coli
    • Choudhury D, Thompson A, Stojanoff V, Langermann S, Pinkner J, et al. (1999) X-ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Escherichia coli. Science 285: 1061–1066.
    • (1999) Science , vol.285 , pp. 1061-1066
    • Choudhury, D.1    Thompson, A.2    Stojanoff, V.3    Langermann, S.4    Pinkner, J.5
  • 4
    • 84871059526 scopus 로고    scopus 로고
    • The Structure of the PapD-PapGII Pilin Complex Reveals an Open and Flexible P5 Pocket
    • Ford B, Verger D, Dodson K, Volkan E, Kostakioti M, et al. (2012) The Structure of the PapD-PapGII Pilin Complex Reveals an Open and Flexible P5 Pocket. J Bacteriol 194: 6390–6397.
    • (2012) J Bacteriol , vol.194 , pp. 6390-6397
    • Ford, B.1    Verger, D.2    Dodson, K.3    Volkan, E.4    Kostakioti, M.5
  • 5
    • 33745195658 scopus 로고    scopus 로고
    • Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism
    • Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, et al. (2006) Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. Mol Cell 22: 831–842.
    • (2006) Mol Cell , vol.22 , pp. 831-842
    • Remaut, H.1    Rose, R.J.2    Hannan, T.J.3    Hultgren, S.J.4    Radford, S.E.5
  • 6
    • 0029738256 scopus 로고    scopus 로고
    • Molecular basis of two subfamilies of immunoglobulin-like chaperones
    • Hung DL, Knight SD, Woods RM, Pinkner JS, Hultgren SJ, (1996) Molecular basis of two subfamilies of immunoglobulin-like chaperones. Embo J 15: 3792–3805.
    • (1996) Embo J , vol.15 , pp. 3792-3805
    • Hung, D.L.1    Knight, S.D.2    Woods, R.M.3    Pinkner, J.S.4    Hultgren, S.J.5
  • 8
    • 9244232327 scopus 로고    scopus 로고
    • Evolutionary and Functional Relationships of Colonization Factor Antigen I and Other Class 5 Adhesive Fimbriae of Entorotoxigenic Escherichia coli
    • Anantha RP, McVeigh AL, Lee LH, Agnew MK, Cassels FJ, et al. (2004) Evolutionary and Functional Relationships of Colonization Factor Antigen I and Other Class 5 Adhesive Fimbriae of Entorotoxigenic Escherichia coli. Infection and Immunity 72: 7190–7201.
    • (2004) Infection and Immunity , vol.72 , pp. 7190-7201
    • Anantha, R.P.1    McVeigh, A.L.2    Lee, L.H.3    Agnew, M.K.4    Cassels, F.J.5
  • 9
    • 0025044255 scopus 로고
    • Gene encoding the major subunit of CS1 pili of human enterotoxigenic Escherichia coli
    • Perez-Casal J, Swartley JS, Scott JR, (1990) Gene encoding the major subunit of CS1 pili of human enterotoxigenic Escherichia coli. Infect Immun 58: 3594–3600.
    • (1990) Infect Immun , vol.58 , pp. 3594-3600
    • Perez-Casal, J.1    Swartley, J.S.2    Scott, J.R.3
  • 10
    • 0029830101 scopus 로고    scopus 로고
    • Assembly proteins of CS1 pili of enterotoxigenic Escherichia coli Molecular
    • Sakellaris H, Balding DP, Scott JR, (1996) Assembly proteins of CS1 pili of enterotoxigenic Escherichia coli Molecular. Microbiology 21: 529–541.
    • (1996) Microbiology , vol.21 , pp. 529-541
    • Sakellaris, H.1    Balding, D.P.2    Scott, J.R.3
  • 11
    • 0033026364 scopus 로고    scopus 로고
    • The level of expression of the minor pilin subunit, CooD, determines the number of CS1 pili assembled on the cell surface of Escherichia coli
    • Sakellaris H, Penumalli VR, Scott JR, (1999) The level of expression of the minor pilin subunit, CooD, determines the number of CS1 pili assembled on the cell surface of Escherichia coli. J Bacteriol 181: 1694–1697.
    • (1999) J Bacteriol , vol.181 , pp. 1694-1697
    • Sakellaris, H.1    Penumalli, V.R.2    Scott, J.R.3
  • 13
    • 0030689826 scopus 로고    scopus 로고
    • CooB plays a chaperone-like role for the proteins involved in formation of CS1 pili of exterotoxigenic Escherichia coli
    • Voegele K, Sakellaris H, Scott JR, (1997) CooB plays a chaperone-like role for the proteins involved in formation of CS1 pili of exterotoxigenic Escherichia coli. Proceedings of the National Academy of Sciences 94: 13257–13261.
    • (1997) Proceedings of the National Academy of Sciences , vol.94 , pp. 13257-13261
    • Voegele, K.1    Sakellaris, H.2    Scott, J.R.3
  • 14
    • 0032989015 scopus 로고    scopus 로고
    • Bacterial adhesins: common themes and variations in architecture and assembly
    • Soto GE, Hultgren SJ, (1999) Bacterial adhesins: common themes and variations in architecture and assembly. Journal of Bacteriology 181: 1059–1071.
    • (1999) Journal of Bacteriology , vol.181 , pp. 1059-1071
    • Soto, G.E.1    Hultgren, S.J.2
  • 15
    • 51049118119 scopus 로고    scopus 로고
    • Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria
    • Fronzes R, Remaut H, Waksman G, (2008) Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria. Embo J 27: 2271–2280.
    • (2008) Embo J , vol.27 , pp. 2271-2280
    • Fronzes, R.1    Remaut, H.2    Waksman, G.3
  • 16
    • 34548288578 scopus 로고    scopus 로고
    • A receptor-binding site as revealed by the crystal structure of CfaE, the CFA/I fimbrial adhesin of enterotoxigenic Escherichia coli
    • Li YF, Poole ST, Rasulova F, McVeigh A, Savarino SJ, et al. (2007) A receptor-binding site as revealed by the crystal structure of CfaE, the CFA/I fimbrial adhesin of enterotoxigenic Escherichia coli. J Biol Chem 282: 23970–23980.
    • (2007) J Biol Chem , vol.282 , pp. 23970-23980
    • Li, Y.F.1    Poole, S.T.2    Rasulova, F.3    McVeigh, A.4    Savarino, S.J.5
  • 18
    • 33846970897 scopus 로고    scopus 로고
    • Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway
    • Poole ST, McVeigh AL, Anantha RP, Lee LH, Akay YM, et al. (2007) Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Mol Microbiol 63: 1372–1384.
    • (2007) Mol Microbiol , vol.63 , pp. 1372-1384
    • Poole, S.T.1    McVeigh, A.L.2    Anantha, R.P.3    Lee, L.H.4    Akay, Y.M.5
  • 19
    • 37349093031 scopus 로고    scopus 로고
    • Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek
    • Nuccio SP, Baumler AJ, (2007) Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek. Microbiol Mol Biol Rev 71: 551–575.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 551-575
    • Nuccio, S.P.1    Baumler, A.J.2
  • 22
    • 79551648713 scopus 로고    scopus 로고
    • Structural and functional characterization of Pseudomonas aeruginosa CupB chaperones
    • Cai X, Wang R, Filloux A, Waksman G, Meng G, (2011) Structural and functional characterization of Pseudomonas aeruginosa CupB chaperones. PLoS One 6: e16583.
    • (2011) PLoS One , vol.6 , pp. e16583
    • Cai, X.1    Wang, R.2    Filloux, A.3    Waksman, G.4    Meng, G.5
  • 23
    • 33947213428 scopus 로고    scopus 로고
    • A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M
    • Zavialov AV, Knight SD, (2007) A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M. Mol Microbiol 64: 153–164.
    • (2007) Mol Microbiol , vol.64 , pp. 153-164
    • Zavialov, A.V.1    Knight, S.D.2
  • 25
    • 79957929732 scopus 로고    scopus 로고
    • Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate
    • Phan G, Remaut H, Wang T, Allen WJ, Pirker KF, et al. (2011) Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature 474: 49–53.
    • (2011) Nature , vol.474 , pp. 49-53
    • Phan, G.1    Remaut, H.2    Wang, T.3    Allen, W.J.4    Pirker, K.F.5
  • 27
    • 70449646172 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG
    • Van Molle I, Moonens K, Garcia-Pino A, Buts L, De Kerpel M, et al. (2009) Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG. J Mol Biol 394: 957–967.
    • (2009) J Mol Biol , vol.394 , pp. 957-967
    • Van Molle, I.1    Moonens, K.2    Garcia-Pino, A.3    Buts, L.4    De Kerpel, M.5
  • 28
    • 84857995188 scopus 로고    scopus 로고
    • Large is fast, small is tight: determinants of speed and affinity in subunit capture by a periplasmic chaperone
    • Yu XD, Fooks LJ, Moslehi-Mohebi E, Tischenko VM, Askarieh G, et al. (2012) Large is fast, small is tight: determinants of speed and affinity in subunit capture by a periplasmic chaperone. J Mol Biol 417: 294–308.
    • (2012) J Mol Biol , vol.417 , pp. 294-308
    • Yu, X.D.1    Fooks, L.J.2    Moslehi-Mohebi, E.3    Tischenko, V.M.4    Askarieh, G.5
  • 29
    • 0030919583 scopus 로고    scopus 로고
    • Influence of the conserved disulphide bond, exposed to the putative binding pocket, on the structure and function of the immunoglobulin-like molecular chaperone Caf1M of Yersinia pestis
    • Zav'yalov VP, Chernovskaya TV, Chapman DA, Karlyshev AV, MacIntyre S, et al. (1997) Influence of the conserved disulphide bond, exposed to the putative binding pocket, on the structure and function of the immunoglobulin-like molecular chaperone Caf1M of Yersinia pestis. Biochem J 324 (Pt 2) 571–578.
    • (1997) Biochem J , vol.324 , pp. 571-578
    • Zav'yalov, V.P.1    Chernovskaya, T.V.2    Chapman, D.A.3    Karlyshev, A.V.4    MacIntyre, S.5
  • 30
    • 11144281811 scopus 로고    scopus 로고
    • Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae: characterization of DraB-DraE complexes
    • Piatek R, Zalewska B, Kolaj O, Ferens M, Nowicki B, et al. (2005) Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae: characterization of DraB-DraE complexes. Infect Immun 73: 135–145.
    • (2005) Infect Immun , vol.73 , pp. 135-145
    • Piatek, R.1    Zalewska, B.2    Kolaj, O.3    Ferens, M.4    Nowicki, B.5
  • 31
    • 0027745982 scopus 로고
    • Structural basis of pilus subunit recognition by the PapD chaperone
    • Kuehn MJ, Ogg DJ, Kihlberg J, Slonim LN, Flemmer K, et al. (1993) Structural basis of pilus subunit recognition by the PapD chaperone. Science 262: 1234–1241.
    • (1993) Science , vol.262 , pp. 1234-1241
    • Kuehn, M.J.1    Ogg, D.J.2    Kihlberg, J.3    Slonim, L.N.4    Flemmer, K.5
  • 32
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone Priming of Pilus Subunit Facilitates a Topological Transition that Drives Fiber Formation
    • Sauer FG, Pinkner JS, Waksman G, Hultgren SJ, (2002) Chaperone Priming of Pilus Subunit Facilitates a Topological Transition that Drives Fiber Formation. Cell 111: 543–551.
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 33
    • 0038820383 scopus 로고    scopus 로고
    • Structure and Biogenesis of the Capsular F1 Antigen from Yersinia pestis: Preserved Folding Energy Drives Fiber Formation
    • Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, et al. (2003) Structure and Biogenesis of the Capsular F1 Antigen from Yersinia pestis: Preserved Folding Energy Drives Fiber Formation. Cell 113: 587–596.
    • (2003) Cell , vol.113 , pp. 587-596
    • Zavialov, A.V.1    Berglund, J.2    Pudney, A.F.3    Fooks, L.J.4    Ibrahim, T.M.5
  • 34
    • 33751534447 scopus 로고    scopus 로고
    • Molecular mechanism of P pilus termination in uropathogenic Escherichia coli
    • Verger D, Miller E, Remaut H, Waksman G, Hultgren S, (2006) Molecular mechanism of P pilus termination in uropathogenic Escherichia coli. EMBO Rep 7: 1228–1232.
    • (2006) EMBO Rep , vol.7 , pp. 1228-1232
    • Verger, D.1    Miller, E.2    Remaut, H.3    Waksman, G.4    Hultgren, S.5
  • 35
    • 34250332241 scopus 로고    scopus 로고
    • FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens
    • Zavialov A, Zav'yalova G, Korpela T, Zav'yalov V, (2007) FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens. FEMS Microbiol Rev 31: 478–514.
    • (2007) FEMS Microbiol Rev , vol.31 , pp. 478-514
    • Zavialov, A.1    Zav'yalova, G.2    Korpela, T.3    Zav'yalov, V.4
  • 36
    • 0032930079 scopus 로고    scopus 로고
    • Structural and functional significance of the FGL sequence of the periplasmic chaperone Caf1M of Yersinia pestis
    • Chapman DA, Zavialov AV, Chernovskaya TV, Karlyshev AV, Zav'yalova GA, et al. (1999) Structural and functional significance of the FGL sequence of the periplasmic chaperone Caf1M of Yersinia pestis. J Bacteriol 181: 2422–2429.
    • (1999) J Bacteriol , vol.181 , pp. 2422-2429
    • Chapman, D.A.1    Zavialov, A.V.2    Chernovskaya, T.V.3    Karlyshev, A.V.4    Zav'yalova, G.A.5
  • 37
    • 0025779451 scopus 로고
    • Positive regulation of colonization factor antigen I (CFA/I) production by enterotoxigenic Escherichia coli producing the colonization factors CS5, CS6, CS7, CS17, PCFO9, PCFO159:H4 and PCFO166
    • Hibberd ML, McConnell MM, Willshaw GA, Smith HR, Rowe B, (1991) Positive regulation of colonization factor antigen I (CFA/I) production by enterotoxigenic Escherichia coli producing the colonization factors CS5, CS6, CS7, CS17, PCFO9, PCFO159:H4 and PCFO166. J Gen Microbiol 137: 1963–1970.
    • (1991) J Gen Microbiol , vol.137 , pp. 1963-1970
    • Hibberd, M.L.1    McConnell, M.M.2    Willshaw, G.A.3    Smith, H.R.4    Rowe, B.5
  • 38
    • 0001083794 scopus 로고    scopus 로고
    • A gentle vapor-diffusion technique for cross-linking of protein crystals for cryocrystallography
    • Lusty CJ, (1999) A gentle vapor-diffusion technique for cross-linking of protein crystals for cryocrystallography. Journal of Applied Crystallography 32: 106–112.
    • (1999) Journal of Applied Crystallography , vol.32 , pp. 106-112
    • Lusty, C.J.1
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography Pt A 276: 307–326.
    • (1997) Macromolecular Crystallography , vol.Pt A 276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution, density modification, and model building
    • Terwilliger T, (2004) SOLVE and RESOLVE: automated structure solution, density modification, and model building. Journal of Synchrotron Radiation 11: 49–52.
    • (2004) Journal of Synchrotron Radiation , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 45
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, (1991) Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47: 110–119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.