메뉴 건너뛰기




Volumn 335, Issue 3, 2004, Pages 775-785

Latent LytM at 1.3 Å resolution

Author keywords

E64, trans epoxysuccinyl L leucylamido (4 guanidino)butane; LytM; Metallopeptidase; Peptidoglycan hydrolase; Proenzyme; Staphylococcus aureus

Indexed keywords

LYSOSTAPHIN; ZINC; BACTERIAL PROTEIN; ENZYME PRECURSOR; LYTM PROTEIN, STAPHYLOCOCCUS AUREUS; PROTEINASE;

EID: 1542705102     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.009     Document Type: Article
Times cited : (102)

References (32)
  • 1
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper N.M. Families of zinc metalloproteases. FEBS Letters. 354:1994;1-6.
    • (1994) FEBS Letters , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 4
    • 0025147543 scopus 로고
    • Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus
    • Li S.L., Norioka S., Sakiyama F. Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus. J. Bacteriol. 172:1990;6506-6511.
    • (1990) J. Bacteriol. , vol.172 , pp. 6506-6511
    • Li, S.L.1    Norioka, S.2    Sakiyama, F.3
  • 5
    • 0025267219 scopus 로고
    • Purification and characterization of an active fragment of the LasA protein from Pseudomonas aeruginosa: Enhancement of elastase activity
    • Peters J.E., Galloway D.R. Purification and characterization of an active fragment of the LasA protein from Pseudomonas aeruginosa: enhancement of elastase activity. J. Bacteriol. 172:1990;2236-2240.
    • (1990) J. Bacteriol. , vol.172 , pp. 2236-2240
    • Peters, J.E.1    Galloway, D.R.2
  • 6
    • 0028961002 scopus 로고
    • The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus
    • DeHart H.P., Heath H.E., Heath L.S., LeBlanc P.A., Sloan G.L. The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. Appl. Environ. Microbiol. 61:1995;1475-1479.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1475-1479
    • Dehart, H.P.1    Heath, H.E.2    Heath, L.S.3    Leblanc, P.A.4    Sloan, G.L.5
  • 7
    • 0035461233 scopus 로고    scopus 로고
    • Self-protection against cell wall hydrolysis in Streptococcus milleri NMSCC 061 and analysis of the millericin B operon
    • Beukes M., Hastings J.W. Self-protection against cell wall hydrolysis in Streptococcus milleri NMSCC 061 and analysis of the millericin B operon. Appl. Environ. Microbiol. 67:2001;3888-3896.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3888-3896
    • Beukes, M.1    Hastings, J.W.2
  • 8
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: Multiple enzymes with multiple functions
    • Smith T.J., Blackman S.A., Foster S.J. Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology. 146:2000;249-262.
    • (2000) Microbiology , vol.146 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 9
    • 0031006866 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of lytM, a unique autolytic gene of Staphylococcus aureus
    • Ramadurai L., Jayaswal R.K. Molecular cloning, sequencing, and expression of lytM, a unique autolytic gene of Staphylococcus aureus. J. Bacteriol. 179:1997;3625-3631.
    • (1997) J. Bacteriol. , vol.179 , pp. 3625-3631
    • Ramadurai, L.1    Jayaswal, R.K.2
  • 10
    • 0032957487 scopus 로고    scopus 로고
    • Characterization of a chromosomally encoded glycylglycine endopeptidase of Staphylococcus aureus
    • Ramadurai L., Lockwood K.J., Nadakavukaren M.J., Jayaswal R.K. Characterization of a chromosomally encoded glycylglycine endopeptidase of Staphylococcus aureus. Microbiology. 145:1999;801-808.
    • (1999) Microbiology , vol.145 , pp. 801-808
    • Ramadurai, L.1    Lockwood, K.J.2    Nadakavukaren, M.J.3    Jayaswal, R.K.4
  • 11
    • 0014103936 scopus 로고
    • Lytic action of lysostaphin on susceptible and resistant strains of Staphylococcus aureus
    • Zygmunt W.A., Browder H.P., Tavormina P.A. Lytic action of lysostaphin on susceptible and resistant strains of Staphylococcus aureus. Can. J. Microbiol. 13:1967;845-853.
    • (1967) Can. J. Microbiol. , vol.13 , pp. 845-853
    • Zygmunt, W.A.1    Browder, H.P.2    Tavormina, P.A.3
  • 12
    • 0031805819 scopus 로고    scopus 로고
    • Lysostaphin treatment of experimental methicillin-resistant Staphylococcus aureus aortic valve endocarditis
    • Climo M.W., Patron R.L., Goldstein B.P., Archer G.L. Lysostaphin treatment of experimental methicillin-resistant Staphylococcus aureus aortic valve endocarditis. Antimicrob. Agents Chemother. 42:1998;1355-1360.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1355-1360
    • Climo, M.W.1    Patron, R.L.2    Goldstein, B.P.3    Archer, G.L.4
  • 13
    • 0030970757 scopus 로고    scopus 로고
    • Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus
    • Thumm G., Gotz F. Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus. Mol. Microbiol. 23:1997;1251-1265.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1251-1265
    • Thumm, G.1    Gotz, F.2
  • 14
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 15
    • 0017387723 scopus 로고
    • Beta-Sheet topology and the relatedness of proteins
    • Richardson J.S. beta-Sheet topology and the relatedness of proteins. Nature. 268:1977;495-500.
    • (1977) Nature , vol.268 , pp. 495-500
    • Richardson, J.S.1
  • 16
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts I.L., Nadassy K., Wodak S.J. Analysis of zinc binding sites in protein crystal structures. Protein Sci. 7:1998;1700-1716.
    • (1998) Protein Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 18
    • 0025303335 scopus 로고
    • Zinc coordination, function and structure of zinc enzymes and other proteins
    • Vallee B.L., Auld D.S. Zinc coordination, function and structure of zinc enzymes and other proteins. Biochemistry. 29:1990;5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 19
    • 0029854956 scopus 로고    scopus 로고
    • A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion
    • Gustin J.K., Kessler E., Ohman D.E. A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion. J. Bacteriol. 178:1996;6608-6617.
    • (1996) J. Bacteriol. , vol.178 , pp. 6608-6617
    • Gustin, J.K.1    Kessler, E.2    Ohman, D.E.3
  • 20
    • 0031046570 scopus 로고    scopus 로고
    • Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1
    • Sugai M., Fujiwara T., Akiyama T., Ohara M., Komatsuzawa H., Inoue S., Suginaka H. Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1. J. Bacteriol. 179:1997;1193-1202.
    • (1997) J. Bacteriol. , vol.179 , pp. 1193-1202
    • Sugai, M.1    Fujiwara, T.2    Akiyama, T.3    Ohara, M.4    Komatsuzawa, H.5    Inoue, S.6    Suginaka, H.7
  • 21
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20:1995;478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 22
    • 0025940839 scopus 로고
    • Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2 Å resolution
    • Liao D.I., Kapadia G., Reddy P., Saier M.H. Jr, Reizer J., Herzberg O. Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2 Å resolution. Biochemistry. 30:1991;9583-9594.
    • (1991) Biochemistry , vol.30 , pp. 9583-9594
    • Liao, D.I.1    Kapadia, G.2    Reddy, P.3    Saier Jr., M.H.4    Reizer, J.5    Herzberg, O.6
  • 23
    • 0020001011 scopus 로고
    • Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution
    • Dideberg O., Charlier P., Dive G., Joris B., Frere J.M., Ghuysen J.M. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution. Nature. 299:1982;469-470.
    • (1982) Nature , vol.299 , pp. 469-470
    • Dideberg, O.1    Charlier, P.2    Dive, G.3    Joris, B.4    Frere, J.M.5    Ghuysen, J.M.6
  • 24
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins"
    • Bode W., Gomis-Ruth F.X., Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins" FEBS Letters. 331:1993;134-140.
    • (1993) FEBS Letters , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 25
    • 0029095760 scopus 로고
    • Structural features of a superfamily of zinc-endopeptidases: The metzincins
    • Stocker W., Bode W. Structural features of a superfamily of zinc-endopeptidases: the metzincins. Curr. Opin. Struct. Biol. 5:1995;383-390.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 383-390
    • Stocker, W.1    Bode, W.2
  • 26
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart H.E., Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl Acad. Sci. USA. 87:1990;5578-5582.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 28
    • 0028805811 scopus 로고
    • Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
    • Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., Fitzgerald P.M., et al. Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein Sci. 4:1995;1966-1976.
    • (1995) Protein Sci. , vol.4 , pp. 1966-1976
    • Becker, J.W.1    Marcy, A.I.2    Rokosz, L.L.3    Axel, M.G.4    Burbaum, J.J.5    Fitzgerald, P.M.6
  • 29
    • 0037194445 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor
    • Feng Y., Likos J.J., Zhu L., Woodward H., Munie G., McDonald J.J., et al. Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor. Biochim. Biophys. Acta. 1598:2002;10-23.
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 10-23
    • Feng, Y.1    Likos, J.J.2    Zhu, L.3    Woodward, H.4    Munie, G.5    McDonald, J.J.6
  • 30
    • 0037172403 scopus 로고    scopus 로고
    • Genome and virulence determinants of high virulence community-acquired MRSA
    • Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., et al. Genome and virulence determinants of high virulence community-acquired MRSA. Lancet. 359:2002;1819-1827.
    • (2002) Lancet , vol.359 , pp. 1819-1827
    • Baba, T.1    Takeuchi, F.2    Kuroda, M.3    Yuzawa, H.4    Aoki, K.5    Oguchi, A.6
  • 31
    • 0029064088 scopus 로고
    • High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli
    • Budisa N., Steipe B., Demange P., Eckerskorn C., Kellermann J., Huber R. High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 230:1995;788-796.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3    Eckerskorn, C.4    Kellermann, J.5    Huber, R.6
  • 32
    • 0024287661 scopus 로고
    • A dye release assay for determination of lysostaphin activity
    • Zhou R., Chen S., Recsei P. A dye release assay for determination of lysostaphin activity. Anal. Biochem. 171:1988;141-144.
    • (1988) Anal. Biochem. , vol.171 , pp. 141-144
    • Zhou, R.1    Chen, S.2    Recsei, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.