메뉴 건너뛰기




Volumn 49, Issue 28, 2010, Pages 5870-5879

Analysis of the crystal structure of the ExsCExsE complex reveals distinctive binding interactions of the pseudomonas aeruginosa type III secretion chaperone ExsC with ExsE and ExsD

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PATHOGENS; BINDING INTERACTION; MEDIATED TRANSCRIPTION; NEW MODEL; P.AERUGINOSA; PSEUDOMONAS AERUGINOSA; SIGNALING CASCADES; SIGNALING PROCESS; TRANSCRIPTIONAL ACTIVATORS; TYPE III SECRETION SYSTEM; TYPE III SECRETIONS; UP-REGULATION;

EID: 77954572518     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100432e     Document Type: Article
Times cited : (22)

References (62)
  • 1
    • 0033023730 scopus 로고    scopus 로고
    • Nosocomial infections in medical intensive care units in the United States. National Nosocomial Infections Surveillance System
    • Richards, M. J., Edwards, J. R., Culver, D. H., and Gaynes, R. P. (1999) Nosocomial infections in medical intensive care units in the United States. National Nosocomial Infections Surveillance System Crit. Care Med. 27, 887-892
    • (1999) Crit. Care Med. , vol.27 , pp. 887-892
    • Richards, M.J.1    Edwards, J.R.2    Culver, D.H.3    Gaynes, R.P.4
  • 2
    • 0029863296 scopus 로고    scopus 로고
    • Ventilator-associated pneumonia due to Pseudomonas aeruginosa
    • Crouch Brewer, S., Wunderink, R. G., Jones, C. B., and Leeper, K. V., Jr. (1996) Ventilator-associated pneumonia due to Pseudomonas aeruginosa Chest 109, 1019-1029
    • (1996) Chest , vol.109 , pp. 1019-1029
    • Crouch Brewer, S.1    Wunderink, R.G.2    Jones, C.B.3    Leeper Jr., K.V.4
  • 3
    • 0000843289 scopus 로고
    • Epithelial cell penetration as an essential step in the pathogenesis of bacillary dysentery
    • Labrec, E. H., Schneider, H., Magnani, T. J., and Formal, S. B. (1964) Epithelial cell penetration as an essential step in the pathogenesis of bacillary dysentery J. Bacteriol. 88, 1503-1518
    • (1964) J. Bacteriol. , vol.88 , pp. 1503-1518
    • Labrec, E.H.1    Schneider, H.2    Magnani, T.J.3    Formal, S.B.4
  • 4
    • 0037397798 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa pneumonia
    • Garau, J. and Gomez, L. (2003) Pseudomonas aeruginosa pneumonia Curr. Opin. Infect. Dis. 16, 135-143
    • (2003) Curr. Opin. Infect. Dis. , vol.16 , pp. 135-143
    • Garau, J.1    Gomez, L.2
  • 6
    • 34248379583 scopus 로고    scopus 로고
    • Opportunistic infections in lung disease: Pseudomonas infections in cystic fibrosis
    • Gomez, M. I. and Prince, A. (2007) Opportunistic infections in lung disease: Pseudomonas infections in cystic fibrosis Curr. Opin. Pharmacol. 7, 244-251
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 244-251
    • Gomez, M.I.1    Prince, A.2
  • 7
    • 0036191393 scopus 로고    scopus 로고
    • Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa
    • Hauser, A. R., Cobb, E., Bodi, M., Mariscal, D., Vallaíes, J., Engel, J. N., and Rello, J. (2002) Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa Crit. Care Med. 30, 521-528
    • (2002) Crit. Care Med. , vol.30 , pp. 521-528
    • Hauser, A.R.1    Cobb, E.2    Bodi, M.3    Mariscal, D.4    Vallaíes, J.5    Engel, J.N.6    Rello, J.7
  • 8
    • 0035137564 scopus 로고    scopus 로고
    • Type III secretion/intoxication system important in virulence of Pseudomonas aeruginosa infections in burns
    • Holder, I. A., Neely, A. N., and Frank, D. W. (2001) Type III secretion/intoxication system important in virulence of Pseudomonas aeruginosa infections in burns Burns: J. Int. Soc. Burn Injuries 27, 129-130
    • (2001) Burns: J. Int. Soc. Burn Injuries , vol.27 , pp. 129-130
    • Holder, I.A.1    Neely, A.N.2    Frank, D.W.3
  • 10
    • 0032907634 scopus 로고    scopus 로고
    • Active and passive immunization with the Pseudomonas v antigen protects against type III intoxication and lung injury
    • Sawa, T., Yahr, T. L., Ohara, M., Kurahashi, K., Gropper, M. A., Wiener-Kronish, J. P., and Frank, D. W. (1999) Active and passive immunization with the Pseudomonas V antigen protects against type III intoxication and lung injury Nat. Med. 5, 392-398
    • (1999) Nat. Med. , vol.5 , pp. 392-398
    • Sawa, T.1    Yahr, T.L.2    Ohara, M.3    Kurahashi, K.4    Gropper, M.A.5    Wiener-Kronish, J.P.6    Frank, D.W.7
  • 11
    • 32444447802 scopus 로고    scopus 로고
    • Keeping their options open: Acute versus persistent infections
    • Furukawa, S., Kuchma, S. L., and O'Toole, G. A. (2006) Keeping their options open: acute versus persistent infections J. Bacteriol. 188, 1211-1217
    • (2006) J. Bacteriol. , vol.188 , pp. 1211-1217
    • Furukawa, S.1    Kuchma, S.L.2    O'Toole, G.A.3
  • 12
    • 7744220530 scopus 로고    scopus 로고
    • A signaling network reciprocally regulates genes associated with acute infection and chronic persistence in Pseudomonas aeruginosa
    • Goodman, A. L., Kulasekara, B., Rietsch, A., Boyd, D., Smith, R. S., and Lory, S. (2004) A signaling network reciprocally regulates genes associated with acute infection and chronic persistence in Pseudomonas aeruginosa Dev. Cell 7, 745-754
    • (2004) Dev. Cell , vol.7 , pp. 745-754
    • Goodman, A.L.1    Kulasekara, B.2    Rietsch, A.3    Boyd, D.4    Smith, R.S.5    Lory, S.6
  • 13
    • 8844219692 scopus 로고    scopus 로고
    • The genetic basis for the commitment to chronic versus acute infection in Pseudomonas aeruginosa
    • Yahr, T. L. and Greenberg, E. P. (2004) The genetic basis for the commitment to chronic versus acute infection in Pseudomonas aeruginosa Mol. Cell 16, 497-498
    • (2004) Mol. Cell , vol.16 , pp. 497-498
    • Yahr, T.L.1    Greenberg, E.P.2
  • 14
    • 59849110833 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa type III effectors in disease
    • Engel, J. and Balachandran, P. (2009) Role of Pseudomonas aeruginosa type III effectors in disease Curr. Opin. Microbiol. 12, 61-66
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 61-66
    • Engel, J.1    Balachandran, P.2
  • 15
    • 0034861186 scopus 로고    scopus 로고
    • Independent and coordinate effects of ADP-ribosyltransferase and GTPase-activating activities of exoenzyme S on HT-29 epithelial cell function
    • Fraylick, J. E., La Rocque, J. R., Vincent, T. S., and Olson, J. C. (2001) Independent and coordinate effects of ADP-ribosyltransferase and GTPase-activating activities of exoenzyme S on HT-29 epithelial cell function Infect. Immun. 69, 5318-5328
    • (2001) Infect. Immun. , vol.69 , pp. 5318-5328
    • Fraylick, J.E.1    La Rocque, J.R.2    Vincent, T.S.3    Olson, J.C.4
  • 16
    • 0036137206 scopus 로고    scopus 로고
    • In vivo rho GTPase-activating protein activity of Pseudomonas aeruginosa cytotoxin ExoS
    • Krall, R., Sun, J., Pederson, K. J., and Barbieri, J. T. (2002) In vivo rho GTPase-activating protein activity of Pseudomonas aeruginosa cytotoxin ExoS Infect. Immun. 70, 360-367
    • (2002) Infect. Immun. , vol.70 , pp. 360-367
    • Krall, R.1    Sun, J.2    Pederson, K.J.3    Barbieri, J.T.4
  • 17
    • 0041355556 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa ExoT ADP-ribosylates CT10 regulator of kinase (Crk) proteins
    • Sun, J. and Barbieri, J. T. (2003) Pseudomonas aeruginosa ExoT ADP-ribosylates CT10 regulator of kinase (Crk) proteins J. Biol. Chem. 278, 32794-32800
    • (2003) J. Biol. Chem. , vol.278 , pp. 32794-32800
    • Sun, J.1    Barbieri, J.T.2
  • 19
    • 0028944578 scopus 로고
    • Transcriptional analysis of the Pseudomonas aeruginosa exoenzyme S structural gene
    • Yahr, T. L., Hovey, A. K., Kulich, S. M., and Frank, D. W. (1995) Transcriptional analysis of the Pseudomonas aeruginosa exoenzyme S structural gene J. Bacteriol. 177, 1169-1178
    • (1995) J. Bacteriol. , vol.177 , pp. 1169-1178
    • Yahr, T.L.1    Hovey, A.K.2    Kulich, S.M.3    Frank, D.W.4
  • 20
    • 0028332195 scopus 로고
    • Transcriptional organization of the trans-regulatory locus which controls exoenzyme S synthesis in Pseudomonas aeruginosa
    • Yahr, T. L. and Frank, D. W. (1994) Transcriptional organization of the trans-regulatory locus which controls exoenzyme S synthesis in Pseudomonas aeruginosa J. Bacteriol. 176, 3832-3838
    • (1994) J. Bacteriol. , vol.176 , pp. 3832-3838
    • Yahr, T.L.1    Frank, D.W.2
  • 21
    • 0028157289 scopus 로고
    • Construction and characterization of chromosomal insertional mutations of the Pseudomonas aeruginosa exoenzyme S trans-regulatory locus
    • Frank, D. W., Nair, G., and Schweizer, H. P. (1994) Construction and characterization of chromosomal insertional mutations of the Pseudomonas aeruginosa exoenzyme S trans-regulatory locus Infect. Immun. 62, 554-563
    • (1994) Infect. Immun. , vol.62 , pp. 554-563
    • Frank, D.W.1    Nair, G.2    Schweizer, H.P.3
  • 22
    • 0030726075 scopus 로고    scopus 로고
    • The exoenzyme S regulon of Pseudomonas aeruginosa
    • Frank, D. W. (1997) The exoenzyme S regulon of Pseudomonas aeruginosa Mol. Microbiol. 26, 621-629
    • (1997) Mol. Microbiol. , vol.26 , pp. 621-629
    • Frank, D.W.1
  • 23
    • 34250318628 scopus 로고    scopus 로고
    • Biochemical characterization of a regulatory cascade controlling transcription of the Pseudomonas aeruginosa type III secretion system
    • Zheng, Z., Chen, G., Joshi, S., Brutinel, E. D., Yahr, T. L., and Chen, L. (2007) Biochemical characterization of a regulatory cascade controlling transcription of the Pseudomonas aeruginosa type III secretion system J. Biol. Chem. 282, 6136-6142
    • (2007) J. Biol. Chem. , vol.282 , pp. 6136-6142
    • Zheng, Z.1    Chen, G.2    Joshi, S.3    Brutinel, E.D.4    Yahr, T.L.5    Chen, L.6
  • 24
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot, C., Hamiaux, C., and Page, A. L. (2003) The various and varying roles of specific chaperones in type III secretion systems Curr. Opin. Microbiol. 6, 7-14
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.L.3
  • 25
    • 0037469577 scopus 로고    scopus 로고
    • The multitalented type III chaperones: All you can do with 15 kDa
    • Feldman, M. F. and Cornelis, G. R. (2003) The multitalented type III chaperones: all you can do with 15 kDa FEMS Microbiol. Lett. 219, 151-158
    • (2003) FEMS Microbiol. Lett. , vol.219 , pp. 151-158
    • Feldman, M.F.1    Cornelis, G.R.2
  • 27
    • 55549100289 scopus 로고    scopus 로고
    • Assignment-free solution NMR method reveals CesT as an unswapped homodimer
    • Rumpel, S., Lakshmi, R., Becker, S., and Zweckstetter, M. (2008) Assignment-free solution NMR method reveals CesT as an unswapped homodimer Protein Sci. 17, 2015-2019
    • (2008) Protein Sci. , vol.17 , pp. 2015-2019
    • Rumpel, S.1    Lakshmi, R.2    Becker, S.3    Zweckstetter, M.4
  • 28
    • 2942543052 scopus 로고    scopus 로고
    • Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity
    • van Eerde, A., Hamiaux, C., Perez, J., Parsot, C., and Dijkstra, B. W. (2004) Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity EMBO Rep. 5, 477-483
    • (2004) EMBO Rep. , vol.5 , pp. 477-483
    • Van Eerde, A.1    Hamiaux, C.2    Perez, J.3    Parsot, C.4    Dijkstra, B.W.5
  • 29
    • 4444333128 scopus 로고    scopus 로고
    • Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis
    • Singer, A. U., Desveaux, D., Betts, L., Chang, J. H., Nimchuk, Z., Grant, S. R., Dangl, J. L., and Sondek, J. (2004) Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis Structure 12, 1669-1681
    • (2004) Structure , vol.12 , pp. 1669-1681
    • Singer, A.U.1    Desveaux, D.2    Betts, L.3    Chang, J.H.4    Nimchuk, Z.5    Grant, S.R.6    Dangl, J.L.7    Sondek, J.8
  • 30
    • 0034753703 scopus 로고    scopus 로고
    • Structure of the Yersinia type III secretory system chaperone SycE
    • Birtalan, S. and Ghosh, P. (2001) Structure of the Yersinia type III secretory system chaperone SycE Nat. Struct. Biol. 8, 974-978
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 974-978
    • Birtalan, S.1    Ghosh, P.2
  • 31
    • 24744442137 scopus 로고    scopus 로고
    • Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT
    • Locher, M., Lehnert, B., Krauss, K., Heesemann, J., Groll, M., and Wilharm, G. (2005) Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT J. Biol. Chem. 280, 31149-31155
    • (2005) J. Biol. Chem. , vol.280 , pp. 31149-31155
    • Locher, M.1    Lehnert, B.2    Krauss, K.3    Heesemann, J.4    Groll, M.5    Wilharm, G.6
  • 32
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C. E. and Galan, J. E. (2001) Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion Nature 414, 77-81
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 33
    • 33344459126 scopus 로고    scopus 로고
    • A common structural motif in the binding of virulence factors to bacterial secretion chaperones
    • Lilic, M., Vujanac, M., and Stebbins, C. E. (2006) A common structural motif in the binding of virulence factors to bacterial secretion chaperones Mol. Cell 21, 653-664
    • (2006) Mol. Cell , vol.21 , pp. 653-664
    • Lilic, M.1    Vujanac, M.2    Stebbins, C.E.3
  • 34
    • 13444303937 scopus 로고    scopus 로고
    • Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis
    • Schubot, F. D., Jackson, M. W., Penrose, K. J., Cherry, S., Tropea, J. E., Plano, G. V., and Waugh, D. S. (2005) Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis J. Mol. Biol. 346, 1147-1161
    • (2005) J. Mol. Biol. , vol.346 , pp. 1147-1161
    • Schubot, F.D.1    Jackson, M.W.2    Penrose, K.J.3    Cherry, S.4    Tropea, J.E.5    Plano, G.V.6    Waugh, D.S.7
  • 35
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan, S. C., Phillips, R. M., and Ghosh, P. (2002) Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens Mol. Cell 9, 971-980
    • (2002) Mol. Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 36
    • 13444295356 scopus 로고    scopus 로고
    • Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2
    • Phan, J., Tropea, J. E., and Waugh, D. S. (2004) Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2 Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 1591-1599
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 1591-1599
    • Phan, J.1    Tropea, J.E.2    Waugh, D.S.3
  • 37
    • 67650133652 scopus 로고    scopus 로고
    • Anti-activator ExsD forms a 1:1 complex with ExsA to inhibit transcription of type III secretion operons
    • Thibault, J., Faudry, E., Ebel, C., Attree, I., and Elsen, S. (2009) Anti-activator ExsD forms a 1:1 complex with ExsA to inhibit transcription of type III secretion operons J. Biol. Chem. 284, 15762-15770
    • (2009) J. Biol. Chem. , vol.284 , pp. 15762-15770
    • Thibault, J.1    Faudry, E.2    Ebel, C.3    Attree, I.4    Elsen, S.5
  • 38
    • 61449116896 scopus 로고    scopus 로고
    • Structural evidence suggests that antiactivator ExsD from Pseudomonas aeruginosa is a DNA binding protein
    • Bernhards, R. C., Jing, X., Vogelaar, N. J., Robinson, H., and Schubot, F. D. (2009) Structural evidence suggests that antiactivator ExsD from Pseudomonas aeruginosa is a DNA binding protein Protein Sci. 18, 503-513
    • (2009) Protein Sci. , vol.18 , pp. 503-513
    • Bernhards, R.C.1    Jing, X.2    Vogelaar, N.J.3    Robinson, H.4    Schubot, F.D.5
  • 39
    • 0036434715 scopus 로고    scopus 로고
    • ExsD is a negative regulator of the Pseudomonas aeruginosa type III secretion regulon
    • McCaw, M. L., Lykken, G. L., Singh, P. K., and Yahr, T. L. (2002) ExsD is a negative regulator of the Pseudomonas aeruginosa type III secretion regulon Mol. Microbiol. 46, 1123-1133
    • (2002) Mol. Microbiol. , vol.46 , pp. 1123-1133
    • McCaw, M.L.1    Lykken, G.L.2    Singh, P.K.3    Yahr, T.L.4
  • 40
    • 3142549041 scopus 로고    scopus 로고
    • A novel anti-anti-activator mechanism regulates expression of the Pseudomonas aeruginosa type III secretion system
    • Dasgupta, N., Lykken, G. L., Wolfgang, M. C., and Yahr, T. L. (2004) A novel anti-anti-activator mechanism regulates expression of the Pseudomonas aeruginosa type III secretion system Mol. Microbiol. 53, 297-308
    • (2004) Mol. Microbiol. , vol.53 , pp. 297-308
    • Dasgupta, N.1    Lykken, G.L.2    Wolfgang, M.C.3    Yahr, T.L.4
  • 41
    • 20344403312 scopus 로고    scopus 로고
    • ExsE, a secreted regulator of type III secretion genes in Pseudomonas aeruginosa
    • Rietsch, A., Vallet-Gely, I., Dove, S. L., and Mekalanos, J. J. (2005) ExsE, a secreted regulator of type III secretion genes in Pseudomonas aeruginosa Proc. Natl. Acad. Sci. U.S.A. 102, 8006-8011
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8006-8011
    • Rietsch, A.1    Vallet-Gely, I.2    Dove, S.L.3    Mekalanos, J.J.4
  • 42
    • 22244459205 scopus 로고    scopus 로고
    • A secreted regulatory protein couples transcription to the secretory activity of the Pseudomonas aeruginosa type III secretion system
    • Urbanowski, M. L., Lykken, G. L., and Yahr, T. L. (2005) A secreted regulatory protein couples transcription to the secretory activity of the Pseudomonas aeruginosa type III secretion system Proc. Natl. Acad. Sci. U.S.A. 102, 9930-9935
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 9930-9935
    • Urbanowski, M.L.1    Lykken, G.L.2    Yahr, T.L.3
  • 43
    • 33749362995 scopus 로고    scopus 로고
    • Characterization of ExsC and ExsD self-association and heterocomplex formation
    • Lykken, G. L., Chen, G., Brutinel, E. D., Chen, L., and Yahr, T. L. (2006) Characterization of ExsC and ExsD self-association and heterocomplex formation J. Bacteriol. 188, 6832-6840
    • (2006) J. Bacteriol. , vol.188 , pp. 6832-6840
    • Lykken, G.L.1    Chen, G.2    Brutinel, E.D.3    Chen, L.4    Yahr, T.L.5
  • 44
    • 28844475180 scopus 로고    scopus 로고
    • Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli
    • Nallamsetty, S., Austin, B. P., Penrose, K. J., and Waugh, D. S. (2005) Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli Protein Sci. 14, 2964-2971
    • (2005) Protein Sci. , vol.14 , pp. 2964-2971
    • Nallamsetty, S.1    Austin, B.P.2    Penrose, K.J.3    Waugh, D.S.4
  • 45
    • 33750451937 scopus 로고    scopus 로고
    • Overproduction, purification, and biochemical characterization of the dual specificity H1 protein phosphatase encoded by variola major virus
    • Tropea, J. E., Phan, J., and Waugh, D. S. (2006) Overproduction, purification, and biochemical characterization of the dual specificity H1 protein phosphatase encoded by variola major virus Protein Expression Purif. 50, 31-36
    • (2006) Protein Expression Purif. , vol.50 , pp. 31-36
    • Tropea, J.E.1    Phan, J.2    Waugh, D.S.3
  • 46
    • 33847290484 scopus 로고    scopus 로고
    • Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems
    • Doublie, S. (2007) Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems Methods Mol. Biol. 363, 91-108
    • (2007) Methods Mol. Biol. , vol.363 , pp. 91-108
    • Doublie, S.1
  • 47
    • 0036808537 scopus 로고    scopus 로고
    • FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification
    • Gattiker, A., Bienvenut, W. V., Bairoch, A., and Gasteiger, E. (2002) FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification Proteomics 2, 1435-1444
    • (2002) Proteomics , vol.2 , pp. 1435-1444
    • Gattiker, A.1    Bienvenut, W.V.2    Bairoch, A.3    Gasteiger, E.4
  • 51
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the steriochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the steriochemical quality of protein structures J. Appl. Crystallogr. 26, 282-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 282-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 53
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • Landau, M., Mayrose, I., Rosenberg, Y., Glaser, F., Martz, E., Pupko, T., and Ben-Tal, N. (2005) ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures Nucleic Acids Res. 33, W299-302
    • (2005) Nucleic Acids Res. , vol.33 , pp. 299-302
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7
  • 54
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm, L., Kaariainen, S., Rosenstrom, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3 Bioinformatics 24, 2780-2781
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 55
    • 51049124329 scopus 로고    scopus 로고
    • The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE
    • Rodgers, L., Gamez, A., Riek, R., and Ghosh, P. (2008) The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE J. Biol. Chem. 283, 20857-20863
    • (2008) J. Biol. Chem. , vol.283 , pp. 20857-20863
    • Rodgers, L.1    Gamez, A.2    Riek, R.3    Ghosh, P.4
  • 56
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot, C., Hamiaux, C., and Page, A. L. (2003) The various and varying roles of specific chaperones in type III secretion systems Curr. Opin. Microbiol. 6, 7-14
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.L.3
  • 57
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • -(1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760 - 763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 59
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A. T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 61
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet, P., Robert, X., and Courcelle, E. (2003) ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins Nucleic Acids Res. 31, 3320-3323
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 62
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A., and Thornton, J. M. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8, 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.