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Volumn 4, Issue 5, 2009, Pages

Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYCLE INHIBITOR FACTOR; CYSTEINE; GLUTAMINE; HISTIDINE; UNCLASSIFIED DRUG;

EID: 65949108013     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005582     Document Type: Article
Times cited : (28)

References (31)
  • 1
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan JE, Wolf-Watz H (2006) Protein delivery into eukaryotic cells by type III secretion machines. Nature 444: 567-573.
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 2
    • 23844495083 scopus 로고    scopus 로고
    • Structural microbiology at the pathogen-host interface
    • Stebbins CE (2005) Structural microbiology at the pathogen-host interface. Cell Microbiol 7: 1227-1236.
    • (2005) Cell Microbiol , vol.7 , pp. 1227-1236
    • Stebbins, C.E.1
  • 3
    • 0035899360 scopus 로고    scopus 로고
    • Structural mimicry in bacterial virulence
    • Stebbins CE, Galan JE (2001) Structural mimicry in bacterial virulence. Nature 412: 701-705.
    • (2001) Nature , vol.412 , pp. 701-705
    • Stebbins, C.E.1    Galan, J.E.2
  • 4
    • 10744230521 scopus 로고    scopus 로고
    • Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycle G2/M transition
    • Marches O, Ledger TN, Boury M, Ohara M, Tu X, et al. (2003) Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycle G2/M transition. Mol Microbiol 50: 1553-1567.
    • (2003) Mol Microbiol , vol.50 , pp. 1553-1567
    • Marches, O.1    Ledger, T.N.2    Boury, M.3    Ohara, M.4    Tu, X.5
  • 5
    • 0034773207 scopus 로고    scopus 로고
    • Type III secretion-dependent cell cycle block caused in HeLa cells by enteropathogenic Escherichia coli O103
    • Nougayrede JP, Boury M, Tasca C, Marches O, Milon A, et al. (2001) Type III secretion-dependent cell cycle block caused in HeLa cells by enteropathogenic Escherichia coli O103. Infect Immun 69: 6785-6795.
    • (2001) Infect Immun , vol.69 , pp. 6785-6795
    • Nougayrede, J.P.1    Boury, M.2    Tasca, C.3    Marches, O.4    Milon, A.5
  • 6
    • 55749091664 scopus 로고    scopus 로고
    • Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclin-dependent kinase inhibitors p21 and p27
    • Samba-Louaka A, Nougayrede JP, Watrin C, Jubelin G, Oswald E, et al. (2008) Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclin-dependent kinase inhibitors p21 and p27 Cell Microbiol 10: 2496-2508.
    • (2008) Cell Microbiol , vol.10 , pp. 2496-2508
    • Samba-Louaka, A.1    Nougayrede, J.P.2    Watrin, C.3    Jubelin, G.4    Oswald, E.5
  • 7
    • 33750577279 scopus 로고    scopus 로고
    • Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway
    • Taieb F, Nougayrede JP, Watrin C, Samba-Louaka A, Oswald E (2006) Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway. Cell Microbiol 8: 1910-1921.
    • (2006) Cell Microbiol , vol.8 , pp. 1910-1921
    • Taieb, F.1    Nougayrede, J.P.2    Watrin, C.3    Samba-Louaka, A.4    Oswald, E.5
  • 10
    • 0032861555 scopus 로고    scopus 로고
    • Yersinia enterocolitica and Yersinia pseudotuberculosis
    • vi
    • Naktin J, Beavis KG (1999) Yersinia enterocolitica and Yersinia pseudotuberculosis. Clin Lab Med 19: 523-536, vi.
    • (1999) Clin Lab Med , vol.19 , pp. 523-536
    • Naktin, J.1    Beavis, K.G.2
  • 11
    • 0027463205 scopus 로고
    • DNA relatedness between Xenorhabdus spp. (Enterobacteriaceae), symbiotic bacteria of entomopathogenic nematodes, and a proposal to transfer Xenorhabdus luminescens to a new genus, Photorhabdus gen. nov
    • Boemare NE, Akhurst RJ, Mourant RG (1993) DNA relatedness between Xenorhabdus spp. (Enterobacteriaceae), symbiotic bacteria of entomopathogenic nematodes, and a proposal to transfer Xenorhabdus luminescens to a new genus, Photorhabdus gen. nov. Int J Syst Bacteriol 43: 249-255.
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 249-255
    • Boemare, N.E.1    Akhurst, R.J.2    Mourant, R.G.3
  • 12
    • 1442299321 scopus 로고    scopus 로고
    • Human infection with Photorhabdus asymbiotica: An emerging bacterial pathogen
    • Gerrard J, Waterfield N, Vohra R, ffrench-Constant R (2004) Human infection with Photorhabdus asymbiotica: an emerging bacterial pathogen. Microbes Infect 6: 229-237.
    • (2004) Microbes Infect , vol.6 , pp. 229-237
    • Gerrard, J.1    Waterfield, N.2    Vohra, R.3    ffrench-Constant, R.4
  • 13
    • 84954358763 scopus 로고    scopus 로고
    • Structure of the cyclomodulin Cif from pathogenic Escherichia coli
    • Hsu Y, Jubelin G, Taieb F, Nougayrede JP, Oswald E, et al. (2008) Structure of the cyclomodulin Cif from pathogenic Escherichia coli. J Mol Biol 384: 465-477.
    • (2008) J Mol Biol , vol.384 , pp. 465-477
    • Hsu, Y.1    Jubelin, G.2    Taieb, F.3    Nougayrede, J.P.4    Oswald, E.5
  • 14
    • 62649121372 scopus 로고    scopus 로고
    • Yao Q, Cui J, Zhu Y, Wang G, Hu L, et al. (2009) A bacterial type III effector family uses the papain-like hydrolytic activity to arrest the host cell cycle. Proc Natl Acad Sci U S A.
    • Yao Q, Cui J, Zhu Y, Wang G, Hu L, et al. (2009) A bacterial type III effector family uses the papain-like hydrolytic activity to arrest the host cell cycle. Proc Natl Acad Sci U S A.
  • 15
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie AG (2006) The integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 62: 48-57.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 16
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62: 72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 17
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4
    • Collaborative Computational Project 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 19
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan KD, Zhang KY (1999) Density modification for macromolecular phase improvement. Prog Biophys Mol Biol 72: 245-270.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 20
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris RJ, Perrakis A, Lamzin VS (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol 374: 229-244.
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 22
  • 23
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5
  • 25
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang ZR, Thomson R, McNeil P, Esnouf RM (2005) RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 21: 3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 26
    • 3843065509 scopus 로고    scopus 로고
    • Identification of the secretion and translocation domain of the enteropathogenic and enterohemorrhagic Escherichia coli effector Cif, using TEM-1 beta-lactamase as a new fluorescence-based reporter
    • Charpentier X, Oswald E (2004) Identification of the secretion and translocation domain of the enteropathogenic and enterohemorrhagic Escherichia coli effector Cif, using TEM-1 beta-lactamase as a new fluorescence-based reporter. J Bacteriol 186: 5486-5495.
    • (2004) J Bacteriol , vol.186 , pp. 5486-5495
    • Charpentier, X.1    Oswald, E.2
  • 27
    • 0025726701 scopus 로고
    • Probing the limits of the DNA breakage-reunion domain of the Escherichia coli DNA gyrase A protein
    • Reece RJ, Maxwell A (1991) Probing the limits of the DNA breakage-reunion domain of the Escherichia coli DNA gyrase A protein. J Biol Chem 266: 3540-3546.
    • (1991) J Biol Chem , vol.266 , pp. 3540-3546
    • Reece, R.J.1    Maxwell, A.2
  • 28
    • 0347719364 scopus 로고    scopus 로고
    • The crystal structure of Pseudomonas avirulence protein AvrPphB: A papain-like fold with a distinct substrate-binding site
    • Zhu M, Shao F, Innes RW, Dixon JE, Xu Z (2004) The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site. Proc Natl Acad Sci U S A 101: 302-307.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 302-307
    • Zhu, M.1    Shao, F.2    Innes, R.W.3    Dixon, J.E.4    Xu, Z.5
  • 30
    • 0037215326 scopus 로고    scopus 로고
    • Position-dependent interactions between cysteine residues and the helix dipole
    • Miranda JJ (2003) Position-dependent interactions between cysteine residues and the helix dipole. Protein Sci 12: 73-81.
    • (2003) Protein Sci , vol.12 , pp. 73-81
    • Miranda, J.J.1
  • 31
    • 85142122881 scopus 로고    scopus 로고
    • Holm L, Kaariainen S, Rosenstrom P, Schenkel A (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24: 2780-2781.
    • Holm L, Kaariainen S, Rosenstrom P, Schenkel A (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24: 2780-2781.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.