메뉴 건너뛰기




Volumn 7, Issue 9, 2011, Pages

Structural and functional studies on the interaction of gspc and gspd in the type ii secretion system

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL PROTEIN; ISOLEUCINE; LEUCINE; METHIONINE; PHENYLALANINE; PROTEIN GSPC; SECRETIN GSPD; TYROSINE; UNCLASSIFIED DRUG; VALINE; MEMBRANE PROTEIN; PEPTIDE HYDROLASE;

EID: 80053453930     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002228     Document Type: Article
Times cited : (78)

References (79)
  • 1
    • 0035019730 scopus 로고    scopus 로고
    • Type II secretion and pathogenesis
    • Sandkvist M, (2001) Type II secretion and pathogenesis. Infect Immun 69: 3523-3535.
    • (2001) Infect Immun , vol.69 , pp. 3523-3535
    • Sandkvist, M.1
  • 2
    • 27844506497 scopus 로고    scopus 로고
    • Type II secretion: a protein secretion system for all seasons
    • Cianciotto NP, (2005) Type II secretion: a protein secretion system for all seasons. Trends Microbiol 13: 581-588.
    • (2005) Trends Microbiol , vol.13 , pp. 581-588
    • Cianciotto, N.P.1
  • 3
    • 34447634995 scopus 로고    scopus 로고
    • Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung
    • DebRoy S, Dao J, Soderberg M, Rossier O, Cianciotto NP, (2006) Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung. Proc Natl Acad Sci U S A 103: 19146-19151.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19146-19151
    • DebRoy, S.1    Dao, J.2    Soderberg, M.3    Rossier, O.4    Cianciotto, N.P.5
  • 4
    • 79955765269 scopus 로고    scopus 로고
    • Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins including three related serine proteases
    • Sikora AE, Zielke RA, Lawrence DA, Andrews PC, Sandkvist M, (2011) Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins including three related serine proteases. J Biol Chem 286: 16555-16566.
    • (2011) J Biol Chem , vol.286 , pp. 16555-16566
    • Sikora, A.E.1    Zielke, R.A.2    Lawrence, D.A.3    Andrews, P.C.4    Sandkvist, M.5
  • 5
    • 0030785514 scopus 로고    scopus 로고
    • General secretion pathway (eps) genes required for toxin secretion and outer membrane biogenesis in Vibrio cholerae
    • Sandkvist M, Michel LO, Hough LP, Morales VM, Bagdasarian M, et al. (1997) General secretion pathway (eps) genes required for toxin secretion and outer membrane biogenesis in Vibrio cholerae. J Bacteriol 179: 6994-7003.
    • (1997) J Bacteriol , vol.179 , pp. 6994-7003
    • Sandkvist, M.1    Michel, L.O.2    Hough, L.P.3    Morales, V.M.4    Bagdasarian, M.5
  • 6
    • 0037076418 scopus 로고    scopus 로고
    • Identification of a protein secretory pathway for the secretion of heat-labile enterotoxin by an enterotoxigenic strain of Escherichia coli
    • Tauschek M, Gorrell RJ, Strugnell RA, Robins-Browne RM, (2002) Identification of a protein secretory pathway for the secretion of heat-labile enterotoxin by an enterotoxigenic strain of Escherichia coli. Proc Natl Acad Sci U S A 99: 7066-7071.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7066-7071
    • Tauschek, M.1    Gorrell, R.J.2    Strugnell, R.A.3    Robins-Browne, R.M.4
  • 7
    • 0023449557 scopus 로고
    • Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae
    • Hirst TR, Holmgren J, (1987) Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae. Proc Natl Acad Sci U S A 84: 7418-7422.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7418-7422
    • Hirst, T.R.1    Holmgren, J.2
  • 8
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux A, (2004) The underlying mechanisms of type II protein secretion. Biochim Biophys Acta 1694: 163-179.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 10
    • 79961171407 scopus 로고    scopus 로고
    • Secretins: dynamic channels for protein transport across membranes
    • Korotkov KV, Gonen T, Hol WGJ, (2011) Secretins: dynamic channels for protein transport across membranes. Trends Biochem Sci 36: 433-443.
    • (2011) Trends Biochem Sci , vol.36 , pp. 433-443
    • Korotkov, K.V.1    Gonen, T.2    Hol, W.G.J.3
  • 11
    • 0037225318 scopus 로고    scopus 로고
    • Structure of the filamentous phage pIV multimer by cryo-electron microscopy
    • Opalka N, Beckmann R, Boisset N, Simon MN, Russel M, et al. (2003) Structure of the filamentous phage pIV multimer by cryo-electron microscopy. J Mol Biol 325: 461-470.
    • (2003) J Mol Biol , vol.325 , pp. 461-470
    • Opalka, N.1    Beckmann, R.2    Boisset, N.3    Simon, M.N.4    Russel, M.5
  • 12
    • 0037389450 scopus 로고    scopus 로고
    • Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy
    • Collins RF, Ford RC, Kitmitto A, Olsen RO, Tonjum T, et al. (2003) Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy. J Bacteriol 185: 2611-2617.
    • (2003) J Bacteriol , vol.185 , pp. 2611-2617
    • Collins, R.F.1    Ford, R.C.2    Kitmitto, A.3    Olsen, R.O.4    Tonjum, T.5
  • 13
    • 79551629041 scopus 로고    scopus 로고
    • Structural characterization of outer membrane components of the type IV pili system in pathogenic Neisseria
    • Jain S, Moscicka KB, Bos MP, Pachulec E, Stuart MC, et al. (2011) Structural characterization of outer membrane components of the type IV pili system in pathogenic Neisseria. PLoS One 6: e16624.
    • (2011) PLoS One , vol.6
    • Jain, S.1    Moscicka, K.B.2    Bos, M.P.3    Pachulec, E.4    Stuart, M.C.5
  • 14
    • 79953227678 scopus 로고    scopus 로고
    • Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27
    • Burkhardt J, Vonck J, Averhoff B, (2011) Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27. J Biol Chem 286: 9977-9984.
    • (2011) J Biol Chem , vol.286 , pp. 9977-9984
    • Burkhardt, J.1    Vonck, J.2    Averhoff, B.3
  • 15
    • 66149119448 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout
    • Hodgkinson JL, Horsley A, Stabat D, Simon M, Johnson S, et al. (2009) Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout. Nat Struct Mol Biol 16: 477-485.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 477-485
    • Hodgkinson, J.L.1    Horsley, A.2    Stabat, D.3    Simon, M.4    Johnson, S.5
  • 16
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • Schraidt O, Marlovits TC, (2011) Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science 331: 1192-1195.
    • (2011) Science , vol.331 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 17
    • 0345306190 scopus 로고    scopus 로고
    • Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella
    • Peabody CR, Chung YJ, Yen MR, Vidal-Ingigliardi D, Pugsley AP, et al. (2003) Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Microbiology 149: 3051-3072.
    • (2003) Microbiology , vol.149 , pp. 3051-3072
    • Peabody, C.R.1    Chung, Y.J.2    Yen, M.R.3    Vidal-Ingigliardi, D.4    Pugsley, A.P.5
  • 18
    • 77955936558 scopus 로고    scopus 로고
    • Architecture of the type II secretion and type IV pilus machineries
    • Ayers M, Howell PL, Burrows LL, (2010) Architecture of the type II secretion and type IV pilus machineries. Future Microbiol 5: 1203-1218.
    • (2010) Future Microbiol , vol.5 , pp. 1203-1218
    • Ayers, M.1    Howell, P.L.2    Burrows, L.L.3
  • 19
    • 27844581702 scopus 로고    scopus 로고
    • Structural insights into the secretin PulD and its trypsin-resistant core
    • Chami M, Guilvout I, Gregorini M, Remigy HW, Muller SA, et al. (2005) Structural insights into the secretin PulD and its trypsin-resistant core. J Biol Chem 280: 37732-37741.
    • (2005) J Biol Chem , vol.280 , pp. 37732-37741
    • Chami, M.1    Guilvout, I.2    Gregorini, M.3    Remigy, H.W.4    Muller, S.A.5
  • 20
    • 77957813869 scopus 로고    scopus 로고
    • Structure of the cholera toxin secretion channel in its closed state
    • Reichow SL, Korotkov KV, Hol WGJ, Gonen T, (2010) Structure of the cholera toxin secretion channel in its closed state. Nat Struct Mol Biol 17: 1226-1232.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1226-1232
    • Reichow, S.L.1    Korotkov, K.V.2    Hol, W.G.J.3    Gonen, T.4
  • 21
    • 0033579546 scopus 로고    scopus 로고
    • The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity
    • Brok R, Van Gelder P, Winterhalter M, Ziese U, Koster AJ, et al. (1999) The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity. J Mol Biol 294: 1169-1179.
    • (1999) J Mol Biol , vol.294 , pp. 1169-1179
    • Brok, R.1    Van Gelder, P.2    Winterhalter, M.3    Ziese, U.4    Koster, A.J.5
  • 22
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • Guilvout I, Chami M, Engel A, Pugsley AP, Bayan N, (2006) Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. EMBO J 25: 5241-5249.
    • (2006) EMBO J , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 23
    • 49349091518 scopus 로고    scopus 로고
    • In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD
    • Guilvout I, Chami M, Berrier C, Ghazi A, Engel A, et al. (2008) In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD. J Mol Biol 382: 13-23.
    • (2008) J Mol Biol , vol.382 , pp. 13-23
    • Guilvout, I.1    Chami, M.2    Berrier, C.3    Ghazi, A.4    Engel, A.5
  • 24
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov KV, Pardon E, Steyaert J, Hol WGJ, (2009) Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 17: 255-265.
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.J.4
  • 25
    • 60949108827 scopus 로고    scopus 로고
    • Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus
    • Lam AY, Pardon E, Korotkov KV, Hol WGJ, Steyaert J, (2009) Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus. J Struct Biol 166: 8-15.
    • (2009) J Struct Biol , vol.166 , pp. 8-15
    • Lam, A.Y.1    Pardon, E.2    Korotkov, K.V.3    Hol, W.G.J.4    Steyaert, J.5
  • 26
    • 79952451439 scopus 로고    scopus 로고
    • Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies
    • Wu M, Park YJ, Pardon E, Turley S, Hayhurst A, et al. (2011) Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies. J Struct Biol 174: 124-136.
    • (2011) J Struct Biol , vol.174 , pp. 124-136
    • Wu, M.1    Park, Y.J.2    Pardon, E.3    Turley, S.4    Hayhurst, A.5
  • 27
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the β2 adrenoceptor
    • Rasmussen SG, Choi HJ, Fung JJ, Pardon E, Casarosa P, et al. (2011) Structure of a nanobody-stabilized active state of the β2 adrenoceptor. Nature 469: 175-180.
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.1    Choi, H.J.2    Fung, J.J.3    Pardon, E.4    Casarosa, P.5
  • 28
    • 28244476414 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli
    • Garcia-Herrero A, Vogel HJ, (2005) Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli. Mol Microbiol 58: 1226-1237.
    • (2005) Mol Microbiol , vol.58 , pp. 1226-1237
    • Garcia-Herrero, A.1    Vogel, H.J.2
  • 29
    • 61849164427 scopus 로고    scopus 로고
    • Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin
    • Leiman PG, Basler M, Ramagopal UA, Bonanno JB, Sauder JM, et al. (2009) Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proc Natl Acad Sci U S A 106: 4154-4159.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4154-4159
    • Leiman, P.G.1    Basler, M.2    Ramagopal, U.A.3    Bonanno, J.B.4    Sauder, J.M.5
  • 30
    • 78449265558 scopus 로고    scopus 로고
    • Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems
    • Nakano N, Kubori T, Kinoshita M, Imada K, Nagai H, (2010) Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems. PLoS Pathog 6: e1001129.
    • (2010) PLoS Pathog , vol.6
    • Nakano, N.1    Kubori, T.2    Kinoshita, M.3    Imada, K.4    Nagai, H.5
  • 31
    • 79958062185 scopus 로고    scopus 로고
    • A Component of the Xanthomonadaceae Type IV Secretion System Combines a VirB7 Motif with a N0 Domain Found in Outer Membrane Transport Proteins
    • Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, et al. (2011) A Component of the Xanthomonadaceae Type IV Secretion System Combines a VirB7 Motif with a N0 Domain Found in Outer Membrane Transport Proteins. PLoS Pathog 7: e1002031.
    • (2011) PLoS Pathog , vol.7
    • Souza, D.P.1    Andrade, M.O.2    Alvarez-Martinez, C.E.3    Arantes, G.M.4    Farah, C.S.5
  • 33
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • Valverde R, Edwards L, Regan L, (2008) Structure and function of KH domains. FEBS J 275: 2712-2726.
    • (2008) FEBS J , vol.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 34
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • 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.
    • (1997) EMBO J , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Baudouy, J.2    Condemine, G.3
  • 35
    • 0036616572 scopus 로고    scopus 로고
    • Identification of XcpP domains that confer functionality and specificity to the Pseudomonas aeruginosa type II secretion apparatus
    • Gerard-Vincent M, Robert V, Ball G, Bleves S, Michel GP, et al. (2002) Identification of XcpP domains that confer functionality and specificity to the Pseudomonas aeruginosa type II secretion apparatus. Mol Microbiol 44: 1651-1665.
    • (2002) Mol Microbiol , vol.44 , pp. 1651-1665
    • Gerard-Vincent, M.1    Robert, V.2    Ball, G.3    Bleves, S.4    Michel, G.P.5
  • 36
    • 0345593398 scopus 로고    scopus 로고
    • Structure-function analysis of XcpP, a component involved in general secretory pathway-dependent protein secretion in Pseudomonas aeruginosa
    • Bleves S, Gerard-Vincent M, Lazdunski A, Filloux A, (1999) Structure-function analysis of XcpP, a component involved in general secretory pathway-dependent protein secretion in Pseudomonas aeruginosa. J Bacteriol 181: 4012-4019.
    • (1999) J Bacteriol , vol.181 , pp. 4012-4019
    • Bleves, S.1    Gerard-Vincent, M.2    Lazdunski, A.3    Filloux, A.4
  • 37
    • 0034090276 scopus 로고    scopus 로고
    • Association of the cytoplasmic membrane protein XpsN with the outer membrane protein XpsD in the type II protein secretion apparatus of Xanthomonas campestris pv. Campestris
    • Lee HM, Wang KC, Liu YL, Yew HY, Chen LY, et al. (2000) Association of the cytoplasmic membrane protein XpsN with the outer membrane protein XpsD in the type II protein secretion apparatus of Xanthomonas campestris pv. Campestris. J Bacteriol 182: 1549-1557.
    • (2000) J Bacteriol , vol.182 , pp. 1549-1557
    • Lee, H.M.1    Wang, K.C.2    Liu, Y.L.3    Yew, H.Y.4    Chen, L.Y.5
  • 38
    • 33748951751 scopus 로고    scopus 로고
    • Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae
    • Korotkov KV, Krumm B, Bagdasarian M, Hol WGJ, (2006) Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae. J Mol Biol 363: 311-321.
    • (2006) J Mol Biol , vol.363 , pp. 311-321
    • Korotkov, K.V.1    Krumm, B.2    Bagdasarian, M.3    Hol, W.G.J.4
  • 40
    • 77952150444 scopus 로고    scopus 로고
    • A 20-residue peptide of the inner membrane protein OutC mediates interaction with two distinct sites of the outer membrane secretin OutD and is essential for the functional type II secretion system in Erwinia chrysanthemi
    • Login FH, Fries M, Wang X, Pickersgill RW, Shevchik VE, (2010) A 20-residue peptide of the inner membrane protein OutC mediates interaction with two distinct sites of the outer membrane secretin OutD and is essential for the functional type II secretion system in Erwinia chrysanthemi. Mol Microbiol 76: 944-955.
    • (2010) Mol Microbiol , vol.76 , pp. 944-955
    • Login, F.H.1    Fries, M.2    Wang, X.3    Pickersgill, R.W.4    Shevchik, V.E.5
  • 41
    • 34250217022 scopus 로고    scopus 로고
    • Double-lanthanide-binding tags for macromolecular crystallographic structure determination
    • Silvaggi NR, Martin LJ, Schwalbe H, Imperiali B, Allen KN, (2007) Double-lanthanide-binding tags for macromolecular crystallographic structure determination. J Am Chem Soc 129: 7114-7120.
    • (2007) J Am Chem Soc , vol.129 , pp. 7114-7120
    • Silvaggi, N.R.1    Martin, L.J.2    Schwalbe, H.3    Imperiali, B.4    Allen, K.N.5
  • 42
    • 33750431393 scopus 로고    scopus 로고
    • The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich fold
    • Golovanov AP, Balasingham S, Tzitzilonis C, Goult BT, Lian LY, et al. (2006) The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich fold. J Mol Biol 364: 186-195.
    • (2006) J Mol Biol , vol.364 , pp. 186-195
    • Golovanov, A.P.1    Balasingham, S.2    Tzitzilonis, C.3    Goult, B.T.4    Lian, L.Y.5
  • 43
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 44
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 45
    • 33746300776 scopus 로고    scopus 로고
    • Protein-protein interaction through β-strand addition
    • Remaut H, Waksman G, (2006) Protein-protein interaction through β-strand addition. Trends Biochem Sci 31: 436-444.
    • (2006) Trends Biochem Sci , vol.31 , pp. 436-444
    • Remaut, H.1    Waksman, G.2
  • 46
    • 0029927929 scopus 로고    scopus 로고
    • Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologues reveals OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via the type II pathway
    • Lindeberg M, Salmond GPC, Collmer A, (1996) Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologues reveals OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via the type II pathway. Mol Microbiol 20: 175-190.
    • (1996) Mol Microbiol , vol.20 , pp. 175-190
    • Lindeberg, M.1    Salmond, G.P.C.2    Collmer, A.3
  • 47
    • 0034034763 scopus 로고    scopus 로고
    • Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE
    • 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.
    • (2000) J Bacteriol , vol.182 , pp. 2142-2152
    • Possot, O.M.1    Vignon, G.2    Bomchil, N.3    Ebel, F.4    Pugsley, A.P.5
  • 48
    • 0034687698 scopus 로고    scopus 로고
    • Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system
    • Jobling MG, Holmes RK, (2000) Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system. Proc Natl Acad Sci U S A 97: 14662-14667.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14662-14667
    • Jobling, M.G.1    Holmes, R.K.2
  • 49
    • 66149092022 scopus 로고    scopus 로고
    • A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system
    • Spreter T, Yip CK, Sanowar S, Andre I, Kimbrough TG, et al. (2009) A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system. Nat Struct Mol Biol 16: 468-476.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 468-476
    • Spreter, T.1    Yip, C.K.2    Sanowar, S.3    Andre, I.4    Kimbrough, T.G.5
  • 50
    • 33846190237 scopus 로고    scopus 로고
    • Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids
    • Camberg JL, Johnson TL, Patrick M, Abendroth J, Hol WGJ, et al. (2007) Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids. EMBO J 26: 19-27.
    • (2007) EMBO J , vol.26 , pp. 19-27
    • Camberg, J.L.1    Johnson, T.L.2    Patrick, M.3    Abendroth, J.4    Hol, W.G.J.5
  • 51
    • 79953223280 scopus 로고    scopus 로고
    • Oligomerization of EpsE coordinates residues from multiple subunits to facilitate ATPase activity
    • Patrick M, Korotkov KV, Hol WGJ, Sandkvist M, (2011) Oligomerization of EpsE coordinates residues from multiple subunits to facilitate ATPase activity. J Biol Chem 286: 10378-10386.
    • (2011) J Biol Chem , vol.286 , pp. 10378-10386
    • Patrick, M.1    Korotkov, K.V.2    Hol, W.G.J.3    Sandkvist, M.4
  • 52
    • 17444370930 scopus 로고    scopus 로고
    • The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae
    • Abendroth J, Murphy P, Sandkvist M, Bagdasarian M, Hol WGJ, (2005) The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae. J Mol Biol 348: 845-855.
    • (2005) J Mol Biol , vol.348 , pp. 845-855
    • Abendroth, J.1    Murphy, P.2    Sandkvist, M.3    Bagdasarian, M.4    Hol, W.G.J.5
  • 53
    • 70350141013 scopus 로고    scopus 로고
    • PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin
    • Ayers M, Sampaleanu LM, Tammam S, Koo J, Harvey H, et al. (2009) PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin. J Mol Biol 394: 128-142.
    • (2009) J Mol Biol , vol.394 , pp. 128-142
    • Ayers, M.1    Sampaleanu, L.M.2    Tammam, S.3    Koo, J.4    Harvey, H.5
  • 54
    • 70350160784 scopus 로고    scopus 로고
    • Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex
    • Sampaleanu LM, Bonanno JB, Ayers M, Koo J, Tammam S, et al. (2009) Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex. J Mol Biol 394: 143-159.
    • (2009) J Mol Biol , vol.394 , pp. 143-159
    • Sampaleanu, L.M.1    Bonanno, J.B.2    Ayers, M.3    Koo, J.4    Tammam, S.5
  • 55
    • 1842686182 scopus 로고    scopus 로고
    • The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold
    • Abendroth J, Rice AE, McLuskey K, Bagdasarian M, Hol WGJ, (2004) The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold. J Mol Biol 338: 585-596.
    • (2004) J Mol Biol , vol.338 , pp. 585-596
    • Abendroth, J.1    Rice, A.E.2    McLuskey, K.3    Bagdasarian, M.4    Hol, W.G.J.5
  • 56
    • 1842487379 scopus 로고    scopus 로고
    • Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism
    • O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WGJ, (2004) Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. Biochemistry 43: 3772-3782.
    • (2004) Biochemistry , vol.43 , pp. 3772-3782
    • O'Neal, C.J.1    Amaya, E.I.2    Jobling, M.G.3    Holmes, R.K.4    Hol, W.G.J.5
  • 57
    • 79955705165 scopus 로고    scopus 로고
    • The binding of cholera toxin to the periplasmic vestibule of the type II secretion channel
    • Reichow SL, Korotkov KV, Gonen M, Sun J, dela Rosa J, et al. (2011) The binding of cholera toxin to the periplasmic vestibule of the type II secretion channel. Channels 5: 215-218.
    • (2011) Channels , vol.5 , pp. 215-218
    • Reichow, S.L.1    Korotkov, K.V.2    Gonen, M.3    Sun, J.4    dela Rosa, J.5
  • 58
    • 0035957511 scopus 로고    scopus 로고
    • The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi
    • Bouley J, Condemine G, Shevchik VE, (2001) The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi. J Mol Biol 308: 205-219.
    • (2001) J Mol Biol , vol.308 , pp. 205-219
    • Bouley, J.1    Condemine, G.2    Shevchik, V.E.3
  • 59
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: Are there distinct domains for multimerization and secretion specificity?
    • Guilvout I, Hardie KR, Sauvonnet N, Pugsley AP, (1999) Genetic dissection of the outer membrane secretin PulD: Are there distinct domains for multimerization and secretion specificity? J Bacteriol 181: 7212-7220.
    • (1999) J Bacteriol , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 60
    • 41149148236 scopus 로고    scopus 로고
    • Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts
    • Klock HE, Koesema EJ, Knuth MW, Lesley SA, (2008) Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts. Proteins 71: 982-994.
    • (2008) Proteins , vol.71 , pp. 982-994
    • Klock, H.E.1    Koesema, E.J.2    Knuth, M.W.3    Lesley, S.A.4
  • 63
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J, (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J Mol Biol 229: 105-124.
    • (1993) J Mol Biol , vol.229 , pp. 105-124
    • van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 66
    • 0034673109 scopus 로고    scopus 로고
    • Camelid heavy-chain variable domains provide efficient combining sites to haptens
    • Spinelli S, Frenken LG, Hermans P, Verrips T, Brown K, et al. (2000) Camelid heavy-chain variable domains provide efficient combining sites to haptens. Biochemistry 39: 1217-1222.
    • (2000) Biochemistry , vol.39 , pp. 1217-1222
    • Spinelli, S.1    Frenken, L.G.2    Hermans, P.3    Verrips, T.4    Brown, K.5
  • 67
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y, (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9: 40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 68
    • 37349110734 scopus 로고    scopus 로고
    • Fitting molecular fragments into electron density
    • Cowtan K, (2008) Fitting molecular fragments into electron density. Acta Crystallogr D Biol Crystallogr 64: 83-89.
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , pp. 83-89
    • Cowtan, K.1
  • 70
    • 70350008224 scopus 로고    scopus 로고
    • Calcium is essential for the major pseudopilin in the type 2 secretion system
    • Korotkov KV, Gray MD, Kreger A, Turley S, Sandkvist M, 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    Gray, M.D.2    Kreger, A.3    Turley, S.4    Sandkvist, M.5
  • 72
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA, (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62: 439-450.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 74
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenstrom P, (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: W545-549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 76
    • 79954580509 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version 1.3r1
    • Schrodinger, LLC
    • Schrodinger, LLC (2010) The PyMOL Molecular Graphics System, Version 1.3r1.
    • (2010)
  • 77
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction
    • Horton RM, Cai ZL, Ho SN, Pease LR, (1990) Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. Biotechniques 8: 528-535.
    • (1990) Biotechniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.L.2    Ho, S.N.3    Pease, L.R.4
  • 78
    • 36749049160 scopus 로고    scopus 로고
    • Compromised outer membrane integrity in Vibrio cholerae type II secretion mutants
    • Sikora AE, Lybarger SR, Sandkvist M, (2007) Compromised outer membrane integrity in Vibrio cholerae type II secretion mutants. J Bacteriol 189: 8484-8495.
    • (2007) J Bacteriol , vol.189 , pp. 8484-8495
    • Sikora, A.E.1    Lybarger, S.R.2    Sandkvist, M.3
  • 79
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.