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Volumn 107, Issue 29, 2010, Pages 13081-13086

Detailed structural and assembly model of the type II secretion pilus from sparse data

Author keywords

Cysteine cross linking; Molecular modeling; Pilus assembly; Protein secretion; Pseudopilus

Indexed keywords

CYSTEINE; PILIN; PULLULANASE;

EID: 77955628595     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1001703107     Document Type: Article
Times cited : (59)

References (31)
  • 2
    • 50049122412 scopus 로고    scopus 로고
    • Towards a systems biology approach to study type II/IV secretion systems
    • Hazes B, Frost L (2008) Towards a systems biology approach to study type II/IV secretion systems. Biochim Biophys Acta 1778:1839-1850.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1839-1850
    • Hazes, B.1    Frost, L.2
  • 3
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet N, Vignon G, Pugsley AP, Gounon P (2000) Pilus formation and protein secretion by the same machinery in Escherichia coli. EMBO J 19:2221-2228. (Pubitemid 30259003)
    • (2000) EMBO Journal , vol.19 , Issue.10 , pp. 2221-2228
    • Sauvonnet, N.1    Vignon, G.2    Pugsley, A.P.3    Gounon, P.4
  • 4
    • 0037853309 scopus 로고    scopus 로고
    • Type IV-like pili formed by the type II secreton: Specificity, composition, bundling, polar localization, and surface presentation of peptides
    • DOI 10.1128/JB.185.11.3416-3428.2003
    • Vignon G, et al. (2003) Type IV-like pili formed by the type II secreton: Specificity, composition, bundling, polar localization, and surface presentation of peptides. J Bacteriol 185:3416-3428. (Pubitemid 36617755)
    • (2003) Journal of Bacteriology , vol.185 , Issue.11 , pp. 3416-3428
    • Vignon, G.1    Kohler, R.2    Larquet, E.3    Giroux, S.4    Prevost, M.-C.5    Roux, P.6    Pugsley, A.P.7
  • 5
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomonas aeruginosa: The pseudopilus is a multifibrillar and adhesive structure
    • Durand E, et al. (2003) Type II protein secretion in Pseudomonas aeruginosa: The pseudopilus is a multifibrillar and adhesive structure. J Bacteriol 185:2749-2758.
    • (2003) J Bacteriol , vol.185 , pp. 2749-2758
    • Durand, E.1
  • 6
    • 0035065972 scopus 로고    scopus 로고
    • An inner membrane platform in the type II secretion machinery of Gram-negative bacteria
    • DOI 10.1093/embo-reports/kve042
    • Py B, Loiseau F, Barras F (2001) An inner membrane platform in the type II secretion machinery of Gram-negative bacteria. EMBO Rep 2:244-248. (Pubitemid 32273305)
    • (2001) EMBO Reports , vol.2 , Issue.3 , pp. 244-248
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 7
    • 33747872707 scopus 로고    scopus 로고
    • Type IV Pilus Structure by Cryo-Electron Microscopy and Crystallography: Implications for Pilus Assembly and Functions
    • DOI 10.1016/j.molcel.2006.07.004, PII S1097276506004813
    • Craig L, et al. (2006) Type IV pilus structure by cryo-electron microscopy and crystallography: Implications for pilus assembly and functions. Mol Cell 23:651-662. (Pubitemid 44292553)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 651-662
    • Craig, L.1    Volkmann, N.2    Arvai, A.S.3    Pique, M.E.4    Yeager, M.5    Egelman, E.6    Tainer, J.A.7
  • 8
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • DOI 10.1093/emboj/16.11.3007
    • Shevchik VE, Robert-Baudouy J, Condemine G (1997) Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J 16:3007-3016. (Pubitemid 27234940)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Baudouy, J.2    Condemine, G.3
  • 9
    • 7644237002 scopus 로고    scopus 로고
    • Structure and assembly of the pseudopilin PulG
    • Kohler R, et al. (2004) Structure and assembly of the pseudopilin PulG. Mol Microbiol 54:647-664.
    • (2004) Mol Microbiol , vol.54 , pp. 647-664
    • Kohler, R.1
  • 10
    • 33947397246 scopus 로고    scopus 로고
    • Signal recognition particle-dependent inner membrane targeting of the PulG pseudopilin component of a type II secretion system
    • DOI 10.1128/JB.01230-06
    • Francetic O, Buddelmeijer N, Lewenza S, Kumamoto CA, Pugsley AP (2007) Signal recognition particle-dependent inner membrane targeting of the PulG pseudopilin component of a type II secretion system. J Bacteriol 189:1783-1793. (Pubitemid 46446141)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1783-1793
    • Francetic, O.1    Buddelmeijer, N.2    Lewenza, S.3    Kumamoto, C.A.4    Pugsley, A.P.5
  • 11
    • 0034034763 scopus 로고    scopus 로고
    • Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE
    • DOI 10.1128/JB.182.8.2142-2152.2000
    • Possot OM, Vignon G, Bomchil N, Ebel F, Pugsley AP (2000) Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE. J Bacteriol 182:2142-2152. (Pubitemid 30183532)
    • (2000) Journal of Bacteriology , vol.182 , Issue.8 , pp. 2142-2152
    • Possot, O.M.1    Vignon, G.2    Bomchil, N.3    Ebel, F.4    Pugsley, A.P.5
  • 12
    • 70350008224 scopus 로고    scopus 로고
    • Calcium is essential for the major pseudopilin in the type 2 secretion system
    • Korotkov KV, et al. (2009) Calcium is essential for the major pseudopilin in the type 2 secretion system. J Biol Chem 284:25466-25470.
    • (2009) J Biol Chem , vol.284 , pp. 25466-25470
    • Korotkov, K.V.1
  • 13
    • 12444272635 scopus 로고    scopus 로고
    • Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin
    • Craig L, et al. (2003) Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin. Mol Cell 11:1139-1150.
    • (2003) Mol Cell , vol.11 , pp. 1139-1150
    • Craig, L.1
  • 14
    • 0025978598 scopus 로고
    • Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly
    • Strom MS, Lory S (1991) Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly. J Biol Chem 266:1656-1664.
    • (1991) J Biol Chem , vol.266 , pp. 1656-1664
    • Strom, M.S.1    Lory, S.2
  • 15
    • 26444506255 scopus 로고    scopus 로고
    • Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca
    • Francetic O, Pugsley AP (2005) Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca. J Bacteriol 187:7045-7055.
    • (2005) J Bacteriol , vol.187 , pp. 7045-7055
    • Francetic, O.1    Pugsley, A.P.2
  • 16
    • 37549005981 scopus 로고    scopus 로고
    • Vibrio cholerae toxin-coregulated pilus structure analyzed by hydrogen/deuterium exchange mass spectrometry
    • Li J, et al. (2008) Vibrio cholerae toxin-coregulated pilus structure analyzed by hydrogen/deuterium exchange mass spectrometry. Structure 16:137-148.
    • (2008) Structure , vol.16 , pp. 137-148
    • Li, J.1
  • 17
    • 36048993418 scopus 로고    scopus 로고
    • Dynamic formation and breaking of disulfide bonds in molecular dynamics simulations with the UNRES force field
    • Chinchio M, Czaplewski C, Liwo A, Oldzej S, Scheraga H (2007) Dynamic formation and breaking of disulfide bonds in molecular dynamics simulations with the UNRES force field. J Chem Theory Comput 3:1236-1248.
    • (2007) J Chem Theory Comput , vol.3 , pp. 1236-1248
    • Chinchio, M.1    Czaplewski, C.2    Liwo, A.3    Oldzej, S.4    Scheraga, H.5
  • 18
    • 67650716743 scopus 로고    scopus 로고
    • The advent of near atomic resolution in single particle electron microscopy
    • Cheng Y, Walz T (2009) The advent of near atomic resolution in single particle electron microscopy. Annu Rev Biochem 78:723-742.
    • (2009) Annu Rev Biochem , vol.78 , pp. 723-742
    • Cheng, Y.1    Walz, T.2
  • 19
    • 33845688257 scopus 로고    scopus 로고
    • Substitutions in the N-terminal alpha helical spine of Neisseria gonorrhoeae pilin affect type IV pilus assembly, dynamics and associated functions
    • Aas FE, et al. (2007) Substitutions in the N-terminal alpha helical spine of Neisseria gonorrhoeae pilin affect type IV pilus assembly, dynamics and associated functions. Mol Microbiol 63:69-85.
    • (2007) Mol Microbiol , vol.63 , pp. 69-85
    • Aas, F.E.1
  • 20
    • 43249092408 scopus 로고    scopus 로고
    • Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system
    • Korotkov KV, Hol WG (2008) Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system. Nat Struct Mol Biol 15:462-468.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 462-468
    • Korotkov, K.V.1    Hol, W.G.2
  • 21
    • 71749119395 scopus 로고    scopus 로고
    • The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus
    • Douzi B, et al. (2009) The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus. J Biol Chem 284:34580-34589.
    • (2009) J Biol Chem , vol.284 , pp. 34580-34589
    • Douzi, B.1
  • 22
    • 43249124991 scopus 로고    scopus 로고
    • The type II secretion arrowhead: The structure of GspI-GspJ-GspK
    • Forest KT (2008) The type II secretion arrowhead: The structure of GspI-GspJ-GspK. Nat Struct Mol Biol 15:428-430.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 428-430
    • Forest, K.T.1
  • 23
    • 72649083410 scopus 로고    scopus 로고
    • Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system
    • Alphonse S, et al. (2010) Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system. J Struct Biol 169:75-80.
    • (2010) J Struct Biol , vol.169 , pp. 75-80
    • Alphonse, S.1
  • 24
    • 56349095598 scopus 로고    scopus 로고
    • SCWRL and MolIDE: Computer programs for side-chain conformation prediction and homology modeling
    • Wang Q, Canutescu AA, Dunbrack RL (2008) SCWRL and MolIDE: Computer programs for side-chain conformation prediction and homology modeling. Nat Protoc 3:1832-1847.
    • (2008) Nat Protoc , vol.3 , pp. 1832-1847
    • Wang, Q.1    Canutescu, A.A.2    Dunbrack, R.L.3
  • 25
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54:905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 26
    • 84962662718 scopus 로고    scopus 로고
    • Protein structure calculation using ambiguous restraints
    • (John Wiley and Sons, New York), 10.1002/9780470034590.emrstm1156
    • Nilges M, Bardiaux B, Malliavin T (2010) Protein structure calculation using ambiguous restraints. Encyclopedia of Magnetic Resonance (John Wiley and Sons, New York), 10.1002/9780470034590.emrstm1156.
    • (2010) Encyclopedia of Magnetic Resonance
    • Nilges, M.1    Bardiaux, B.2    Malliavin, T.3
  • 27
    • 0035501755 scopus 로고    scopus 로고
    • Protein molecular dynamics with the generalized Born/ACE solvent model
    • Calimet N, Schaefer M, Simonson T (2001) Protein molecular dynamics with the generalized Born/ACE solvent model. Proteins 45:144-158.
    • (2001) Proteins , vol.45 , pp. 144-158
    • Calimet, N.1    Schaefer, M.2    Simonson, T.3
  • 28
    • 0347062349 scopus 로고    scopus 로고
    • Reintroducing electrostatics into protein X-ray structure refinement: Bulk solvent treated as a dielectric continuum
    • Moulinier L, Case DA, Simonson T (2003) Reintroducing electrostatics into protein X-ray structure refinement: Bulk solvent treated as a dielectric continuum. Acta Crystallogr D Biol Crystallogr 59:2094-2103.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 2094-2103
    • Moulinier, L.1    Case, D.A.2    Simonson, T.3
  • 29
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy and minimization and dynamics calculations
    • Brooks B, et al. (1983) CHARMM: A program for macromolecular energy and minimization and dynamics calculations. J Comput Chem 4:187-217.
    • (1983) J Comput Chem , vol.4 , pp. 187-217
    • Brooks, B.1


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