메뉴 건너뛰기




Volumn 586, Issue 19, 2012, Pages 3193-3199

Crystal structure of type VI effector Tse1 from Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; ANTITOXIN; PEPTIDOGLYCAN AMIDASE; TSI1 PROTEIN; UNCLASSIFIED DRUG;

EID: 84866626957     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.06.036     Document Type: Article
Times cited : (22)

References (30)
  • 1
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen
    • C.K. Stover Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen Nature 406 2000 959 964
    • (2000) Nature , vol.406 , pp. 959-964
    • Stover, C.K.1
  • 2
    • 33750582837 scopus 로고    scopus 로고
    • The impact of quorum sensing and swarming motility on Pseudomonas aeruginosa biofilm formation is nutritionally conditional
    • J.D. Shrout, D.L. Chopp, C.L. Just, M. Hentzer, M. Givskov, and M.R. Parsek The impact of quorum sensing and swarming motility on Pseudomonas aeruginosa biofilm formation is nutritionally conditional Mol. Microbiol. 62 2006 1264 1277
    • (2006) Mol. Microbiol. , vol.62 , pp. 1264-1277
    • Shrout, J.D.1    Chopp, D.L.2    Just, C.L.3    Hentzer, M.4    Givskov, M.5    Parsek, M.R.6
  • 3
    • 48449086943 scopus 로고    scopus 로고
    • The bacterial type VI secretion machine: Yet another player for protein transport across membranes
    • A. Filloux, A. Hachani, and S. Bleves The bacterial type VI secretion machine: yet another player for protein transport across membranes Microbiology 154 2008 1570 1583
    • (2008) Microbiology , vol.154 , pp. 1570-1583
    • Filloux, A.1    Hachani, A.2    Bleves, S.3
  • 4
    • 59849101362 scopus 로고    scopus 로고
    • The type VI secretion system: Translocation of effectors and effector-domains
    • S. Pukatzki, S.B. McAuley, and S.T. Miyata The type VI secretion system: translocation of effectors and effector-domains Curr. Opin. Microbiol. 12 2009 11 17
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 11-17
    • Pukatzki, S.1    McAuley, S.B.2    Miyata, S.T.3
  • 5
    • 77958182267 scopus 로고    scopus 로고
    • Type VI secretion: Not just for pathogenesis anymore
    • A.J. Jani, and P.A. Cotter Type VI secretion: not just for pathogenesis anymore Cell Host Microbe 8 2010 2 6
    • (2010) Cell Host Microbe , vol.8 , pp. 2-6
    • Jani, A.J.1    Cotter, P.A.2
  • 6
    • 74049096227 scopus 로고    scopus 로고
    • A typeVI secretion system of Pseudomonas aeruginosa targets a toxin to bacteria
    • R.D. Hood A typeVI secretion system of Pseudomonas aeruginosa targets a toxin to bacteria Cell Host Microbe 7 2010 25 37
    • (2010) Cell Host Microbe , vol.7 , pp. 25-37
    • Hood, R.D.1
  • 8
    • 80054759036 scopus 로고    scopus 로고
    • Regulation of growth and death in Escherichia coli by toxin-antitoxin systems
    • Y. Yamaguchi, and M. Inouye Regulation of growth and death in Escherichia coli by toxin-antitoxin systems Nat. Rev. Microbiol. 9 2011 779 790
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 779-790
    • Yamaguchi, Y.1    Inouye, M.2
  • 9
    • 77949367813 scopus 로고    scopus 로고
    • A conserved mode of protein recognition and binding in a ParD -ParE toxin-antitoxin complex
    • K.M. Dalton, and S. Crosson A conserved mode of protein recognition and binding in a ParD -ParE toxin-antitoxin complex Biochemistry 49 2010 2205 2215
    • (2010) Biochemistry , vol.49 , pp. 2205-2215
    • Dalton, K.M.1    Crosson, S.2
  • 11
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 12
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • P.D. Adams PHENIX: a comprehensive Python-based system for macromolecular structure solution Acta Cryst. D 66 2010 213 221
    • (2010) Acta Cryst. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 14
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • V.B. Chen MolProbity: all-atom structure validation for macromolecular crystallography Acta Cryst. D 66 2010 12 21
    • (2010) Acta Cryst. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 15
    • 53149133857 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein
    • P. Kumar, B. Issac, E.J. Dodson, J.P. Turkenburg, and S.C. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein J. Mol. Biol. 383 2008 482 493
    • (2008) J. Mol. Biol. , vol.383 , pp. 482-493
    • Kumar, P.1    Issac, B.2    Dodson, E.J.3    Turkenburg, J.P.4    Mande, S.C.5
  • 17
    • 84861170138 scopus 로고    scopus 로고
    • Structural basis for Type VI secretion effector recognition by a cognate immunity protein
    • M. Li Structural basis for Type VI secretion effector recognition by a cognate immunity protein PLoS Pathog. 8 2012 e1002613
    • (2012) PLoS Pathog. , vol.8 , pp. 1002613
    • Li, M.1
  • 18
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes
    • V. Anantharaman, and L. Aravind Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes Genome Biol. 4 2003 R11
    • (2003) Genome Biol. , vol.4 , pp. 11
    • Anantharaman, V.1    Aravind, L.2
  • 19
    • 0038403691 scopus 로고    scopus 로고
    • The CHAP domain: A large family of amidases including GSP amidase and peptidoglycan hydrolases
    • A. Bateman, and N.D. Rawlings The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases Trends Biochem. Sci. 28 2003 234 237
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 234-237
    • Bateman, A.1    Rawlings, N.D.2
  • 20
    • 0037727706 scopus 로고    scopus 로고
    • Amidase domains from bacterial and phage autolysins define a family of g -d,l-glutamate-specific amidohydrolases
    • D.J. Rigden, M.J. Jedrzejas, and M.Y. Galperin Amidase domains from bacterial and phage autolysins define a family of g -d,l-glutamate-specific amidohydrolases. Trends Biochem. Sci. 28 2003 230 234
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 230-234
    • Rigden, D.J.1    Jedrzejas, M.J.2    Galperin, M.Y.3
  • 21
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • A.R. Frand, J.W. Cuozzo, and C.A. Kaiser Pathways for protein disulphide bond formation Trends Cell Biol. 10 2000 203 210
    • (2000) Trends Cell Biol. , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 23
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • J. Dundas, Z. Ouyang, J. Tseng, A. Binkowski, Y. Turpaz, and J. Liang CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues Nucleic Acids Res. 34 2006 W116 W118
    • (2006) Nucleic Acids Res. , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 24
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.J. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acid Res. 22 1994 4673 4680
    • (1994) Nucleic Acid Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.J.2    Gibson, T.J.3
  • 25
  • 26
    • 77958061197 scopus 로고    scopus 로고
    • Structure of the γ-d-glutamyl-l-diamino acid endopeptidase YkfC from Bacillus cereus in complex with l-Ala-γ-d-Glu: Insights into substrate recognition by NlpC/P60 cysteine peptidases
    • Q.P. Xu Structure of the γ-d-glutamyl-l-diamino acid endopeptidase YkfC from Bacillus cereus in complex with l-Ala-γ-d-Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases Acta Cryst. F 66 2010 1354 1364
    • (2010) Acta Cryst. F , vol.66 , pp. 1354-1364
    • Xu, Q.P.1
  • 27
    • 51849165615 scopus 로고    scopus 로고
    • Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: Structural evidence for a novel cysteine peptidase catalytic triad
    • J.M. Aramini Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad Biochemistry 47 2008 9715 9717
    • (2008) Biochemistry , vol.47 , pp. 9715-9717
    • Aramini, J.M.1
  • 28
    • 59649104674 scopus 로고    scopus 로고
    • Structural basis of murein peptide specificity of a γ-d-glutamyl-l- diamino acid endopeptidase
    • Q.P. Xu Structural basis of murein peptide specificity of a γ-d-glutamyl-l-diamino acid endopeptidase Structure 17 2009 303 313
    • (2009) Structure , vol.17 , pp. 303-313
    • Xu, Q.P.1
  • 29
    • 80053309991 scopus 로고    scopus 로고
    • Peptidoglycan remodeling in Mycobacterium tuberculosis: Comparison of structures and catalytic activities of RipA and RipB
    • D. Both, G.And. Schneider, and R. Schnell Peptidoglycan remodeling in Mycobacterium tuberculosis: comparison of structures and catalytic activities of RipA and RipB J. Mol. Biol. 413 2011 247 260
    • (2011) J. Mol. Biol. , vol.413 , pp. 247-260
    • Both, D.1    Schneider, G.2    Schnell, R.3
  • 30
    • 77956331325 scopus 로고    scopus 로고
    • Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation
    • A. Ruggiero, D. Marasco, F. Squeglia, S. Soldini, E. Pedone, C. Pedone, and R. Berisio Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation Structure 18 2010 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.