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Volumn 6, Issue 4, 2011, Pages

The structure of Helicobacter pylori HP0310 reveals an atypical peptidoglycan deacetylase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; PEPTIDOGLYCAN DEACETYLASE; PROTEIN HP0310; UNCLASSIFIED DRUG; AMIDASE; PEPTIDE; PEPTIDOGLYCAN; POLYSACCHARIDE DEACETYLASE; SOLVENT;

EID: 79955734425     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019207     Document Type: Article
Times cited : (18)

References (31)
  • 1
    • 33846526208 scopus 로고    scopus 로고
    • A critical role for peptidoglycan N-deacetylation in listeria evasion from the host innate immune system
    • Boneca IG, Dussurget O, Cabanes D, Nahori MA, Sousa S, et al. (2007) A critical role for peptidoglycan N-deacetylation in listeria evasion from the host innate immune system. Proc Natl Acad Sci U S A 104 (3): 997-1002.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.3 , pp. 997-1002
    • Boneca, I.G.1    Dussurget, O.2    Cabanes, D.3    Nahori, M.A.4    Sousa, S.5
  • 2
    • 33244472793 scopus 로고    scopus 로고
    • Signalling pathways and molecular interactions of NOD1 and NOD2
    • Strober W, Murray PJ, Kitani A, Watanabe T, (2006) Signalling pathways and molecular interactions of NOD1 and NOD2. Nat Rev Immunol 6 (1): 9-20.
    • (2006) Nat Rev Immunol , vol.6 , Issue.1 , pp. 9-20
    • Strober, W.1    Murray, P.J.2    Kitani, A.3    Watanabe, T.4
  • 3
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E, Tschopp J, Karin M, (2006) Intracellular pattern recognition receptors in the host response. Nature 442 (7098): 39-44.
    • (2006) Nature , vol.442 , Issue.7098 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 4
    • 78049430106 scopus 로고    scopus 로고
    • Peptidoglycan deacetylation in Helicobacter pylori contributes to bacterial survival by mitigating host immune responses
    • Wang G, Maier SE, Lo LF, Maier G, Dosi S, et al. (2010) Peptidoglycan deacetylation in Helicobacter pylori contributes to bacterial survival by mitigating host immune responses. Infect Immun 78 (11): 4660-4666.
    • (2010) Infect Immun , vol.78 , Issue.11 , pp. 4660-4666
    • Wang, G.1    Maier, S.E.2    Lo, L.F.3    Maier, G.4    Dosi, S.5
  • 5
    • 65449142126 scopus 로고    scopus 로고
    • Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori
    • Wang G, Olczak A, Forsberg LS, Maier RJ, (2009) Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori. J Biol Chem 284 (11): 6790-6800.
    • (2009) J Biol Chem , vol.284 , Issue.11 , pp. 6790-6800
    • Wang, G.1    Olczak, A.2    Forsberg, L.S.3    Maier, R.J.4
  • 6
    • 27344441825 scopus 로고    scopus 로고
    • Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor
    • Blair DE, Schuttelkopf AW, MacRae JI, van Aalten DM, (2005) Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc Natl Acad Sci U S A 102 (43): 15429-15434.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.43 , pp. 15429-15434
    • Blair, D.E.1    Schuttelkopf, A.W.2    MacRae, J.I.3    van Aalten, D.M.4
  • 9
    • 3142568420 scopus 로고    scopus 로고
    • Structures of bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine
    • Blair DE, van Aalten DM, (2004) Structures of bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine. FEBS Lett 570 (1-3): 13-19.
    • (2004) FEBS Lett , vol.570 , Issue.1-3 , pp. 13-19
    • Blair, D.E.1    van Aalten, D.M.2
  • 10
    • 0027440362 scopus 로고
    • Protein-structure comparison by alignment of distance matrices
    • Holm L, Sander C, (1993) Protein-structure comparison by alignment of distance matrices. J Mol Biol 233 (1): 123-138.
    • (1993) J Mol Biol , vol.233 , Issue.1 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 11
    • 53149095833 scopus 로고    scopus 로고
    • Logical identification of an allantoinase analog (PuuE) recruited from polysaccharide deacetylases
    • 10.1074/jbc.M801195200
    • Ramazzina I, Cendron L, Folli C, Berni R, Monteverdi D, et al. (2008) Logical identification of an allantoinase analog (PuuE) recruited from polysaccharide deacetylases. J Biol Chem 283 (34): 23295-23304 10.1074/jbc.M801195200.
    • (2008) J Biol Chem , vol.283 , Issue.34 , pp. 23295-23304
    • Ramazzina, I.1    Cendron, L.2    Folli, C.3    Berni, R.4    Monteverdi, D.5
  • 12
    • 0037155881 scopus 로고    scopus 로고
    • The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein
    • Luthy L, Grutter MG, Mittl PR, (2002) The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein. J Biol Chem 277 (12): 10187-10193.
    • (2002) J Biol Chem , vol.277 , Issue.12 , pp. 10187-10193
    • Luthy, L.1    Grutter, M.G.2    Mittl, P.R.3
  • 14
    • 0023219970 scopus 로고
    • Putrescine and cadaverine are constituents of peptidoglycan in Veillonella alcalescens and Veillonella parvula
    • Kamio Y, Nakamura K, (1987) Putrescine and cadaverine are constituents of peptidoglycan in Veillonella alcalescens and Veillonella parvula. J Bacteriol 169 (6): 2881-2884.
    • (1987) J Bacteriol , vol.169 , Issue.6 , pp. 2881-2884
    • Kamio, Y.1    Nakamura, K.2
  • 15
    • 0034254598 scopus 로고    scopus 로고
    • Recognition of Chitooligosaccharides and Their N-Acetyl Groups by Putative Subsites of Chitin Deacetylase from a Deuteromycete, Colletotrichum lindemuthianum
    • Tokuyasu K, Mitsutomi M, Yamaguchi I, Hayashi K, Mori Y, (2000) Recognition of Chitooligosaccharides and Their N-Acetyl Groups by Putative Subsites of Chitin Deacetylase from a Deuteromycete, Colletotrichum lindemuthianum. Biochemistry 39: 8837-8843.
    • (2000) Biochemistry , vol.39 , pp. 8837-8843
    • Tokuyasu, K.1    Mitsutomi, M.2    Yamaguchi, I.3    Hayashi, K.4    Mori, Y.5
  • 16
    • 0042330067 scopus 로고    scopus 로고
    • Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: an investigation using steady-state kinetic analysis and MS
    • Hekmat O, Tokuyasu K, Withers SG, (2003) Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: an investigation using steady-state kinetic analysis and MS. Biochem J 374: 369-380.
    • (2003) Biochem J , vol.374 , pp. 369-380
    • Hekmat, O.1    Tokuyasu, K.2    Withers, S.G.3
  • 17
    • 34447545490 scopus 로고    scopus 로고
    • Direct analysis of the extracellular proteome from two strains of Helicobacter pylori
    • Smith TG, Lim JM, Weinberg MV, Wells L, Hoover TR, (2007) Direct analysis of the extracellular proteome from two strains of Helicobacter pylori. Proteomics 7 (13): 2240-2245.
    • (2007) Proteomics , vol.7 , Issue.13 , pp. 2240-2245
    • Smith, T.G.1    Lim, J.M.2    Weinberg, M.V.3    Wells, L.4    Hoover, T.R.5
  • 18
    • 53149153132 scopus 로고    scopus 로고
    • Characterization of structural variations in the peptidoglycan of vancomycin-susceptible Enterococcus faecium: Understanding glycopeptide-antibiotic binding sites using mass spectrometry
    • Patti GJ, Chen J, Schaefer J, Gross ML, (2008) Characterization of structural variations in the peptidoglycan of vancomycin-susceptible Enterococcus faecium: Understanding glycopeptide-antibiotic binding sites using mass spectrometry. J Am Soc Mass Spectrom 19 (10): 1467-1475.
    • (2008) J Am Soc Mass Spectrom , vol.19 , Issue.10 , pp. 1467-1475
    • Patti, G.J.1    Chen, J.2    Schaefer, J.3    Gross, M.L.4
  • 19
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie AGW, (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.W.1
  • 20
    • 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
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50 (Pt 5): 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.Pt 5 , pp. 760-763
  • 27
    • 0000243829 scopus 로고
    • Procheck - a program to check the stereochemical quality of protein structures
    • Laskowski RA, Macarthur MW, Moss DS, Thornton JM, (1993) Procheck- a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F, (1999) ESPript: Analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (4): 305-308.
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 29
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 (22): 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M, (1987) The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol Biol Evol 4 (4): 406-425.
    • (1987) Mol Biol Evol , vol.4 , Issue.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.