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Volumn 426, Issue 1, 2014, Pages 169-184

Structures of a bifunctional cell wall hydrolase CwlT containing a novel bacterial lysozyme and an NlpC/P60 dl-endopeptidase

Author keywords

bacterial lysozyme; bifunctional cell wall lysin; muramidase; NlpC P60 endopeptidase; Tn916 family conjugative transposons

Indexed keywords

CWIT PROTEIN; GLYCAN; GLYCOSIDASE; GLYCOSYLTRANSFERASE; HYDROLASE; LYSOZYME; PROTEINASE; UNCLASSIFIED DRUG; WATER;

EID: 84890855791     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.09.011     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 66249099218 scopus 로고    scopus 로고
    • A modular master on the move: The Tn916 family of mobile genetic elements
    • A.P. Roberts, and P. Mullany A modular master on the move: the Tn916 family of mobile genetic elements Trends Microbiol 17 2009 251 258
    • (2009) Trends Microbiol , vol.17 , pp. 251-258
    • Roberts, A.P.1    Mullany, P.2
  • 2
    • 79960946351 scopus 로고    scopus 로고
    • Tn916-like genetic elements: A diverse group of modular mobile elements conferring antibiotic resistance
    • A.P. Roberts, and P. Mullany Tn916-like genetic elements: a diverse group of modular mobile elements conferring antibiotic resistance FEMS Microbiol Rev 35 2011 856 871
    • (2011) FEMS Microbiol Rev , vol.35 , pp. 856-871
    • Roberts, A.P.1    Mullany, P.2
  • 4
    • 73849149870 scopus 로고    scopus 로고
    • Conjugative transfer of the integrative and conjugative element ICEBs1 from Bacillus subtilis likely initiates at the donor cell pole
    • E. Grohmann Conjugative transfer of the integrative and conjugative element ICEBs1 from Bacillus subtilis likely initiates at the donor cell pole J Bacteriol 192 2010 23 25
    • (2010) J Bacteriol , vol.192 , pp. 23-25
    • Grohmann, E.1
  • 5
    • 45549087223 scopus 로고    scopus 로고
    • Identification and characterization of novel cell wall hydrolase CwlT: A two-domain autolysin exhibiting N-acetylmuramidase and dl-endopeptidase activities
    • T. Fukushima, T. Kitajima, H. Yamaguchi, Q. Ouyang, K. Furuhata, and H. Yamamoto et al. Identification and characterization of novel cell wall hydrolase CwlT: a two-domain autolysin exhibiting N-acetylmuramidase and dl-endopeptidase activities J Biol Chem 283 2008 11117 11125
    • (2008) J Biol Chem , vol.283 , pp. 11117-11125
    • Fukushima, T.1    Kitajima, T.2    Yamaguchi, H.3    Ouyang, Q.4    Furuhata, K.5    Yamamoto, H.6
  • 6
    • 0035114563 scopus 로고    scopus 로고
    • Use of a whole genome approach to identify vaccine molecules affording protection against Streptococcus pneumoniae infection
    • T.M. Wizemann, J.H. Heinrichs, J.E. Adamou, A.L. Erwin, C. Kunsch, and G.H. Choi et al. Use of a whole genome approach to identify vaccine molecules affording protection against Streptococcus pneumoniae infection Infect Immun 69 2001 1593 1598
    • (2001) Infect Immun , vol.69 , pp. 1593-1598
    • Wizemann, T.M.1    Heinrichs, J.H.2    Adamou, J.E.3    Erwin, A.L.4    Kunsch, C.5    Choi, G.H.6
  • 7
    • 6044223543 scopus 로고    scopus 로고
    • Lactobacillus plantarum bacteriophage LP65: A new member of the SPO1-like genus of the family Myoviridae
    • S. Chibani-Chennoufi, M.L. Dillmann, L. Marvin-Guy, S. Rami-Shojaei, and H. Brussow Lactobacillus plantarum bacteriophage LP65: a new member of the SPO1-like genus of the family Myoviridae J Bacteriol 186 2004 7069 7083
    • (2004) J Bacteriol , vol.186 , pp. 7069-7083
    • Chibani-Chennoufi, S.1    Dillmann, M.L.2    Marvin-Guy, L.3    Rami-Shojaei, S.4    Brussow, H.5
  • 8
    • 2942614873 scopus 로고    scopus 로고
    • Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax
    • A.R. Hoffmaster, J. Ravel, D.A. Rasko, G.D. Chapman, M.D. Chute, and C.K. Marston et al. Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax Proc Natl Acad Sci USA 101 2004 8449 8454
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8449-8454
    • Hoffmaster, A.R.1    Ravel, J.2    Rasko, D.A.3    Chapman, G.D.4    Chute, M.D.5    Marston, C.K.6
  • 9
    • 0242606104 scopus 로고    scopus 로고
    • The vanG glycopeptide resistance operon from Enterococcus faecalis revisited
    • F. Depardieu, M.G. Bonora, P.E. Reynolds, and P. Courvalin The vanG glycopeptide resistance operon from Enterococcus faecalis revisited Mol Microbiol 50 2003 931 948
    • (2003) Mol Microbiol , vol.50 , pp. 931-948
    • Depardieu, F.1    Bonora, M.G.2    Reynolds, P.E.3    Courvalin, P.4
  • 10
    • 77957372885 scopus 로고    scopus 로고
    • Dissemination of an Enterococcus Inc18-like vanA plasmid associated with vancomycin-resistant Staphylococcus aureus
    • W. Zhu, P.R. Murray, W.C. Huskins, J.A. Jernigan, L.C. McDonald, and N.C. Clark et al. Dissemination of an Enterococcus Inc18-like vanA plasmid associated with vancomycin-resistant Staphylococcus aureus Antimicrob Agents Chemother 54 2010 4314 4320
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 4314-4320
    • Zhu, W.1    Murray, P.R.2    Huskins, W.C.3    Jernigan, J.A.4    McDonald, L.C.5    Clark, N.C.6
  • 11
    • 59649104674 scopus 로고    scopus 로고
    • Structural basis of murein peptide specificity of a γ-d-glutamyl-l- diamino acid endopeptidase
    • Q. Xu, S. Sudek, D. McMullan, M.D. Miller, B. Geierstanger, and D.H. Jones et al. 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.1    Sudek, S.2    McMullan, D.3    Miller, M.D.4    Geierstanger, B.5    Jones, D.H.6
  • 12
    • 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. Xu, P. Abdubek, T. Astakhova, H.L. Axelrod, C. Bakolitsa, and X. Cai et al. 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 Crystallogr Sect F Struct Biol Cryst Commun 66 2010 1354 1364
    • (2010) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.66 , pp. 1354-1364
    • Xu, Q.1    Abdubek, P.2    Astakhova, T.3    Axelrod, H.L.4    Bakolitsa, C.5    Cai, X.6
  • 13
    • 79960670480 scopus 로고    scopus 로고
    • Structural analysis of papain-like NlpC/P60 superfamily enzymes with a circularly permuted topology reveals potential lipid binding sites
    • Q. Xu, N.D. Rawlings, H.J. Chiu, L. Jaroszewski, H.E. Klock, and M.W. Knuth et al. Structural analysis of papain-like NlpC/P60 superfamily enzymes with a circularly permuted topology reveals potential lipid binding sites PLoS One 6 2011 e22013
    • (2011) PLoS One , vol.6 , pp. 22013
    • Xu, Q.1    Rawlings, N.D.2    Chiu, H.J.3    Jaroszewski, L.4    Klock, H.E.5    Knuth, M.W.6
  • 14
    • 0035925904 scopus 로고    scopus 로고
    • Whole genome sequencing of meticillin-resistant Staphylococcus aureus
    • M. Kuroda, T. Ohta, I. Uchiyama, T. Baba, H. Yuzawa, and I. Kobayashi et al. Whole genome sequencing of meticillin-resistant Staphylococcus aureus Lancet 357 2001 1225 1240
    • (2001) Lancet , vol.357 , pp. 1225-1240
    • Kuroda, M.1    Ohta, T.2    Uchiyama, I.3    Baba, T.4    Yuzawa, H.5    Kobayashi, I.6
  • 15
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction - The Phobius web server
    • L. Kall, A. Krogh, and E.L. Sonnhammer Advantages of combined transmembrane topology and signal peptide prediction - the Phobius web server Nucleic Acids Res 35 2007 W429 W432
    • (2007) Nucleic Acids Res , vol.35
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 18
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J Mol Biol 372 2007 774 797
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 20
    • 55049135817 scopus 로고    scopus 로고
    • Bacteriophage lysins as effective antibacterials
    • V.A. Fischetti Bacteriophage lysins as effective antibacterials Curr Opin Microbiol 11 2008 393 400
    • (2008) Curr Opin Microbiol , vol.11 , pp. 393-400
    • Fischetti, V.A.1
  • 21
    • 84869078754 scopus 로고    scopus 로고
    • On the mechanism of peptidoglycan binding and cleavage by the endo-specific lytic transglycosylase MltE from Escherichia coli
    • G. Fibriansah, F.I. Gliubich, and A.M. Thunnissen On the mechanism of peptidoglycan binding and cleavage by the endo-specific lytic transglycosylase MltE from Escherichia coli Biochemistry 51 2012 9164 9177
    • (2012) Biochemistry , vol.51 , pp. 9164-9177
    • Fibriansah, G.1    Gliubich, F.I.2    Thunnissen, A.M.3
  • 22
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • L. Holm, and P. Rosenstrom Dali server: conservation mapping in 3D Nucleic Acids Res 38 2010 W545 W549
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 23
    • 67650960649 scopus 로고    scopus 로고
    • Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism
    • R. Helland, R.L. Larsen, S. Finstad, P. Kyomuhendo, and A.N. Larsen Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism Cell Mol Life Sci 66 2009 2585 2598
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2585-2598
    • Helland, R.1    Larsen, R.L.2    Finstad, S.3    Kyomuhendo, P.4    Larsen, A.N.5
  • 24
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • K. Tamura, D. Peterson, N. Peterson, G. Stecher, M. Nei, and S. Kumar MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol Biol Evol 28 2011 2731 2739
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 25
    • 78649737514 scopus 로고    scopus 로고
    • Structural relationships in the lysozyme superfamily: Significant evidence for glycoside hydrolase signature motifs
    • A. Wohlkonig, J. Huet, Y. Looze, and R. Wintjens Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs PLoS One 5 2010 e15388
    • (2010) PLoS One , vol.5 , pp. 15388
    • Wohlkonig, A.1    Huet, J.2    Looze, Y.3    Wintjens, R.4
  • 26
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • D.L. Zechel, and S.G. Withers Glycosidase mechanisms: anatomy of a finely tuned catalyst Acc Chem Res 33 2000 11 18
    • (2000) Acc Chem Res , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 27
    • 0033529853 scopus 로고    scopus 로고
    • Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site
    • R. Kuroki, L.H. Weaver, and B.W. Matthews Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site Proc Natl Acad Sci USA 96 1999 8949 8954
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8949-8954
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 28
    • 0035943705 scopus 로고    scopus 로고
    • A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 Å resolution
    • A. Rau, T. Hogg, R. Marquardt, and R. Hilgenfeld A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 Å resolution J Biol Chem 276 2001 31994 31999
    • (2001) J Biol Chem , vol.276 , pp. 31994-31999
    • Rau, A.1    Hogg, T.2    Marquardt, R.3    Hilgenfeld, R.4
  • 29
    • 84863613709 scopus 로고    scopus 로고
    • Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes
    • S.I. Patzer, R. Albrecht, V. Braun, and K. Zeth Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes J Biol Chem 287 2012 23381 23396
    • (2012) J Biol Chem , vol.287 , pp. 23381-23396
    • Patzer, S.I.1    Albrecht, R.2    Braun, V.3    Zeth, K.4
  • 30
    • 0033609769 scopus 로고    scopus 로고
    • High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment
    • E.J. van Asselt, A.M. Thunnissen, and B.W. Dijkstra High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment J Mol Biol 291 1999 877 898
    • (1999) J Mol Biol , vol.291 , pp. 877-898
    • Van Asselt, E.J.1    Thunnissen, A.M.2    Dijkstra, B.W.3
  • 31
    • 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, P. Rossi, Y.J. Huang, L. Zhao, M. Jiang, and M. Maglaqui et al. 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    Rossi, P.2    Huang, Y.J.3    Zhao, L.4    Jiang, M.5    Maglaqui, M.6
  • 32
    • 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
  • 33
    • 41149148236 scopus 로고    scopus 로고
    • Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts
    • H.E. Klock, E.J. Koesema, M.W. Knuth, and S.A. Lesley Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts Proteins 71 2008 982 994
    • (2008) Proteins , vol.71 , pp. 982-994
    • Klock, H.E.1    Koesema, E.J.2    Knuth, M.W.3    Lesley, S.A.4
  • 34
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • T.N. Petersen, S. Brunak, G. von Heijne, and H. Nielsen SignalP 4.0: discriminating signal peptides from transmembrane regions Nat Methods 8 2011 785 786
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 35
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • G.D. Van Duyne, R.F. Standaert, P.A. Karplus, S.L. Schreiber, and J. Clardy Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin J Mol Biol 229 1993 105 124
    • (1993) J Mol Biol , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 37
    • 0037015054 scopus 로고    scopus 로고
    • Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline
    • S.A. Lesley, P. Kuhn, A. Godzik, A.M. Deacon, I. Mathews, and A. Kreusch et al. Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline Proc Natl Acad Sci USA 99 2002 11664 11669
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11664-11669
    • Lesley, S.A.1    Kuhn, P.2    Godzik, A.3    Deacon, A.M.4    Mathews, I.5    Kreusch, A.6
  • 38
    • 0036896410 scopus 로고    scopus 로고
    • An automated system to mount cryo-cooled protein crystals on a synchrotron beamline, using compact samples cassettes and a small-scale robot
    • A.E. Cohen, P.J. Ellis, M.D. Miller, A.M. Deacon, and R.P. Phizackerley An automated system to mount cryo-cooled protein crystals on a synchrotron beamline, using compact samples cassettes and a small-scale robot J Appl Crystallogr 35 2002 720 726
    • (2002) J Appl Crystallogr , vol.35 , pp. 720-726
    • Cohen, A.E.1    Ellis, P.J.2    Miller, M.D.3    Deacon, A.M.4    Phizackerley, R.P.5
  • 42
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • G. Bricogne, C. Vonrhein, C. Flensburg, M. Schiltz, and W. Paciorek Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0 Acta Crystallogr Sect D Biol Crystallogr 59 2003 2023 2030
    • (2003) Acta Crystallogr Sect D Biol Crystallogr , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 43
    • 37349110734 scopus 로고    scopus 로고
    • Fitting molecular fragments into electron density
    • K. Cowtan Fitting molecular fragments into electron density Acta Crystallogr Sect D Biol Crystallogr 64 2008 83 89
    • (2008) Acta Crystallogr Sect D Biol Crystallogr , vol.64 , pp. 83-89
    • Cowtan, K.1
  • 47
    • 3242886389 scopus 로고    scopus 로고
    • MolProbity: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • I.W. Davis, L.W. Murray, J.S. Richardson, and D.C. Richardson MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes Nucleic Acids Res 32 2004 W615 W619
    • (2004) Nucleic Acids Res , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 48
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • A.W. Schuttelkopf, and D.M. van Aalten PRODRG: a tool for high-throughput crystallography of protein-ligand complexes Acta Crystallogr Sect D Biol Crystallogr 60 2004 1355 1363
    • (2004) Acta Crystallogr Sect D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2


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