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Volumn 287, Issue 32, 2012, Pages 26911-26920

Structural insights into the Pseudomonas aeruginosa type VI virulence effector tse1 bacteriolysis and self-protection mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBACTERIAL AGENT; BIACORE; CATALYTIC SITES; FUNCTIONAL PERFORMANCE; IMMUNITY PROTEINS; MOLECULAR PLATFORM; P.AERUGINOSA; PEPTIDE SUBSTRATES; PHYSIOLOGICAL SUBSTRATE; PSEUDOMONAS AERUGINOSA; SECRETION SYSTEMS; STRUCTURAL BASIS; STRUCTURAL INSIGHTS; STRUCTURAL MECHANISMS; SUBSTRATE-BINDING SITES;

EID: 84864544191     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.368043     Document Type: Article
Times cited : (43)

References (34)
  • 1
    • 0035449070 scopus 로고    scopus 로고
    • Can bacterial interference prevent infection?
    • DOI 10.1016/S0966-842X(01)02132-1, PII S0966842X01021321
    • Reid, G., Howard, J., and Gan, B. S. (2001) Can bacterial interference prevent infection? Trends Microbiol. 9, 424-428 (Pubitemid 32844328)
    • (2001) Trends in Microbiology , vol.9 , Issue.9 , pp. 424-428
    • Reid, G.1    Howard, J.2    Gan, B.S.3
  • 2
    • 12344250668 scopus 로고    scopus 로고
    • Human polymicrobial infections
    • DOI 10.1016/S0140-6736(05)17745-9, PII S0140673605177459
    • Brogden, K. A., Guthmiller, J. M., and Taylor, C. E. (2005) Human polymicrobial infections. Lancet 365, 253-255 (Pubitemid 40138019)
    • (2005) Lancet , vol.365 , Issue.9455 , pp. 253-255
    • Brogden, K.A.1    Guthmiller, J.M.2    Taylor, C.E.3
  • 4
    • 73949111750 scopus 로고    scopus 로고
    • Bacterial competition. Surviving and thriving in the microbial jungle
    • Hibbing, M. E., Fuqua, C., Parsek, M. R., and Peterson, S. B. (2010) Bacterial competition. Surviving and thriving in the microbial jungle. Nat. Rev. Microbiol. 8, 15-25
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 15-25
    • Hibbing, M.E.1    Fuqua, C.2    Parsek, M.R.3    Peterson, S.B.4
  • 6
    • 48649107476 scopus 로고    scopus 로고
    • The type VI secretion toolkit
    • Cascales, E. (2008) The type VI secretion toolkit. EMBO Rep. 9, 735-741
    • (2008) EMBO Rep. , vol.9 , pp. 735-741
    • Cascales, E.1
  • 7
    • 77958182267 scopus 로고    scopus 로고
    • Type VI secretion. Not just for pathogenesis anymore
    • Jani, A. J., and Cotter, P. A. (2010) Type VI secretion. Not just for pathogenesis anymore. Cell Host Microbe 8, 2-6
    • (2010) Cell Host Microbe , vol.8 , pp. 2-6
    • Jani, A.J.1    Cotter, P.A.2
  • 8
    • 78649326935 scopus 로고    scopus 로고
    • What is type VI secretion doing in all those bugs?
    • Schwarz, S., Hood, R. D., and Mougous, J. D. (2010) What is type VI secretion doing in all those bugs? Trends Microbiol. 18, 531-537
    • (2010) Trends Microbiol. , vol.18 , pp. 531-537
    • Schwarz, S.1    Hood, R.D.2    Mougous, J.D.3
  • 12
    • 61849155151 scopus 로고    scopus 로고
    • The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system
    • Pell, L. G., Kanelis, V., Donaldson, L. W., Howell, P. L., and Davidson, A. R. (2009) The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc. Natl. Acad. Sci. U.S.A. 106, 4160-4165
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4160-4165
    • Pell, L.G.1    Kanelis, V.2    Donaldson, L.W.3    Howell, P.L.4    Davidson, A.R.5
  • 14
    • 63149199451 scopus 로고    scopus 로고
    • Structural similarity of tailed phages and pathogenic bacterial secretion systems
    • Kanamaru, S. (2009) Structural similarity of tailed phages and pathogenic bacterial secretion systems. Proc. Natl. Acad. Sci. U.S.A. 106, 4067-4068
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4067-4068
    • Kanamaru, S.1
  • 16
    • 79960648176 scopus 로고    scopus 로고
    • Type VI secretion delivers bacteriolytic effectors to target cells
    • Russell, A. B., Hood, R. D., Bui, N. K., LeRoux, M., Vollmer, W., and Mougous, J. D. (2011) Type VI secretion delivers bacteriolytic effectors to target cells. Nature 475, 343-347
    • (2011) Nature , vol.475 , pp. 343-347
    • Russell, A.B.1    Hood, R.D.2    Bui, N.K.3    LeRoux, M.4    Vollmer, W.5    Mougous, J.D.6
  • 17
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 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
  • 22
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • DOI 10.1093/bioinformatics/15.4.305
    • Gouet, P., Courcelle, E., Stuart, D. I., and Métoz, F. (1999) ESPript. Analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (Pubitemid 29213756)
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 23
    • 77954288774 scopus 로고    scopus 로고
    • Dali server. Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server. Conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 27
    • 77956331325 scopus 로고    scopus 로고
    • Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation
    • Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., and Berisio, R. (2010) Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation. Structure 18, 1184-1190
    • (2010) Structure , vol.18 , pp. 1184-1190
    • Ruggiero, A.1    Marasco, D.2    Squeglia, F.3    Soldini, S.4    Pedone, E.5    Pedone, C.6    Berisio, R.7
  • 28
    • 80053309991 scopus 로고    scopus 로고
    • Peptidoglycan remodeling in Mycobacterium tuberculosis. Comparison of structures and catalytic activities of RipA and RipB
    • Böth, D., Schneider, G., and Schnell, R. (2011) Peptidoglycan remodeling in Mycobacterium tuberculosis. Comparison of structures and catalytic activities of RipA and RipB. J. Mol. Biol. 413, 247-260
    • (2011) J. Mol. Biol. , vol.413 , pp. 247-260
    • Böth, D.1    Schneider, G.2    Schnell, R.3
  • 29
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features, and biochemical diversity of the NlpC/P60 superfamily of enzymes
    • Anantharaman, V., and Aravind, L. (2003) Evolutionary history, structural features, and biochemical diversity of the NlpC/P60 superfamily of enzymes. Genome Biol. 4, R11
    • (2003) Genome Biol. , vol.4
    • Anantharaman, V.1    Aravind, L.2
  • 30
    • 57349169308 scopus 로고    scopus 로고
    • Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue
    • Nakajima, Y., Ito, K., Toshima, T., Egawa, T., Zheng, H., Oyama, H., Wu, Y. F., Takahashi, E., Kyono, K., and Yoshimoto, T. (2008) Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue. J. Bacteriol. 190, 7819-7829
    • (2008) J. Bacteriol. , vol.190 , pp. 7819-7829
    • Nakajima, Y.1    Ito, K.2    Toshima, T.3    Egawa, T.4    Zheng, H.5    Oyama, H.6    Wu, Y.F.7    Takahashi, E.8    Kyono, K.9    Yoshimoto, T.10
  • 31
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A. C., and Ménard, R. (1994) Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 244, 486-500
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Ménard, R.2
  • 32
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)
    • DOI 10.1128/MMBR.00027-07
    • Park, J. T., and Uehara, T. (2008) How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol. Mol. Biol. Rev. 72, 211-227 (Pubitemid 351822290)
    • (2008) Microbiology and Molecular Biology Reviews , vol.72 , Issue.2 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 33
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: Multiple enzymes with multiple functions
    • Smith, T. J., Blackman, S. A., and Foster, S. J. (2000) Autolysins of Bacillus subtilis. Multiple enzymes with multiple functions. Microbiology 146, 249-262 (Pubitemid 30099199)
    • (2000) Microbiology , vol.146 , Issue.2 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.