메뉴 건너뛰기




Volumn 6, Issue 9, 1998, Pages 1185-1193

Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 Å resolution

Author keywords

Aureolysin; Metalloproteinases; Staphylococcus aureus; Thermolysin

Indexed keywords

AMINO ACID SEQUENCE; AUREOLYSIN; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; METALLOPROTEINASE; STAPHYLOCOCCUS AUREUS;

EID: 0032530707     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00118-X     Document Type: Article
Times cited : (76)

References (35)
  • 1
    • 0027140429 scopus 로고
    • Bacterial extracellular zinc-containing metalloproinases
    • Hase, C.C. & Finkelstein, RA. (1993). Bacterial extracellular zinc-containing metalloproinases. Microbiol. Rev. 57, 823-837.
    • (1993) Microbiol. Rev. , vol.57 , pp. 823-837
    • Hase, C.C.1    Finkelstein, R.A.2
  • 3
    • 0024278094 scopus 로고
    • Crystal structure of neutral protease from Bacillus cereus refined at 3.0 a resolution and comparison with the homologous but more thermostable enzyme thermolysin
    • Pauptit, R.A., Karlsson, R., Picot, D., Jenkins, J.A., Niklaus-Reimer, A.-S. & Jansonius, J.N. (1988). Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin. J. Mol. Biol. 199, 525-537.
    • (1988) J. Mol. Biol. , vol.199 , pp. 525-537
    • Pauptit, R.A.1    Karlsson, R.2    Picot, D.3    Jenkins, J.A.4    Niklaus-Reimer, A.-S.5    Jansonius, J.N.6
  • 4
    • 0025906404 scopus 로고
    • Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5 Å resolution
    • Thayer, M.M., Flaherty, K.M. & McKay, D.B. (1991). Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5 Å resolution. J. Biol. Chem. 266, 2864-2871.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2864-2871
    • Thayer, M.M.1    Flaherty, K.M.2    McKay, D.B.3
  • 5
    • 0021744255 scopus 로고
    • An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides
    • Hangauer, D.G., Monzingo, A.F. & Matthews, B.W. (1984). An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides. Biochemistry 23, 5730-5741.
    • (1984) Biochemistry , vol.23 , pp. 5730-5741
    • Hangauer, D.G.1    Monzingo, A.F.2    Matthews, B.W.3
  • 6
    • 0031041656 scopus 로고    scopus 로고
    • Activation of human matrix metalloproteinases by various bacterial proteinases
    • Okamoto, T. et al., & Maeda, H. (1997). Activation of human matrix metalloproteinases by various bacterial proteinases. J. Biol. Chem. 272, 6059-6066.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6059-6066
    • Okamoto, T.1    Maeda, H.2
  • 7
    • 0026549140 scopus 로고
    • Virulence factors of the family Legionellaceae
    • Dowling, J.A., Saha, A.K. & Glew, R.A. (1992). Virulence factors of the family Legionellaceae. Microbiol. Rev. 56, 32-60.
    • (1992) Microbiol. Rev. , vol.56 , pp. 32-60
    • Dowling, J.A.1    Saha, A.K.2    Glew, R.A.3
  • 8
    • 0030218050 scopus 로고    scopus 로고
    • Vibrio cholerae hemagglutinin/protease (HA/protease) causes morphological changes in cultured epithelial cells and perturbs their paracellular barrier function
    • Wu, Z., Milton, D., Nybom, P., Sjo, A., Magnusson, K.E. (1996). Vibrio cholerae hemagglutinin/protease (HA/protease) causes morphological changes in cultured epithelial cells and perturbs their paracellular barrier function. Microb. Pathog. 21, 111-123.
    • (1996) Microb. Pathog. , vol.21 , pp. 111-123
    • Wu, Z.1    Milton, D.2    Nybom, P.3    Sjo, A.4    Magnusson, K.E.5
  • 9
    • 0029858955 scopus 로고    scopus 로고
    • In vitro proteolytic processing and activation of the recombinant precursor of E1 tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases
    • Nagamune, K., Yamamoto, K., Naka, A., Matsuyama, J., Miwatani, T. & Honda, T. (1996) In vitro proteolytic processing and activation of the recombinant precursor of E1 tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases. Infect. Immun. 64, 4655-4658.
    • (1996) Infect. Immun. , vol.64 , pp. 4655-4658
    • Nagamune, K.1    Yamamoto, K.2    Naka, A.3    Matsuyama, J.4    Miwatani, T.5    Honda, T.6
  • 10
    • 0026332855 scopus 로고
    • Vibrio cholerae hemagglutinin/protease, colonial variation, virulence, and detachment
    • Finkelstein, R.A., Boesman-Finkelstein, M., Chang, Y. & Hase, C.C. (1992). Vibrio cholerae hemagglutinin/protease, colonial variation, virulence, and detachment. Infect. Immun. 60, 472-478.
    • (1992) Infect. Immun. , vol.60 , pp. 472-478
    • Finkelstein, R.A.1    Boesman-Finkelstein, M.2    Chang, Y.3    Hase, C.C.4
  • 11
    • 0014868209 scopus 로고
    • Formation of bacteriolytic enzymes in batch and continuous culture of Staphylococcus aureus
    • Arvidson, S.O., Holme, T. & Wadstrom, T. (1970). Formation of bacteriolytic enzymes in batch and continuous culture of Staphylococcus aureus. J. Bacteriol. 104, 227-233.
    • (1970) J. Bacteriol. , vol.104 , pp. 227-233
    • Arvidson, S.O.1    Holme, T.2    Wadstrom, T.3
  • 12
    • 0017640208 scopus 로고
    • Occurrence of an extracellular serine proteinase among Staphylococcus aureus strains
    • Björklind, A. & Arvidson, S.O. (1977). Occurrence of an extracellular serine proteinase among Staphylococcus aureus strains. Acta Pathol. Microbiol. Immunol. Scand [B], 85, 277-280.
    • (1977) Acta Pathol. Microbiol. Immunol. Scand [B] , vol.85 , pp. 277-280
    • Björklind, A.1    Arvidson, S.O.2
  • 13
    • 0023031993 scopus 로고
    • The inactivation of human α-1-proteinase inhibitor by proteinases from Staphylococcus aureus
    • Potempa, J., Watorek, W. & Travis, J. (1986). The inactivation of human α-1-proteinase inhibitor by proteinases from Staphylococcus aureus. J. Biol. Chem. 261, 14330-14334.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14330-14334
    • Potempa, J.1    Watorek, W.2    Travis, J.3
  • 14
    • 0025833842 scopus 로고
    • Proteolytic inactivation of a-1-anti-chymotrypsin. Sites of cleavage and generation of chemotactic activity
    • Potempa, J., Fedak, D., Dubin, A., Mast, A. & Travis, J. (1991). Proteolytic inactivation of a-1-anti-chymotrypsin. Sites of cleavage and generation of chemotactic activity. J. Biol. Chem. 266, 21482-21487.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21482-21487
    • Potempa, J.1    Fedak, D.2    Dubin, A.3    Mast, A.4    Travis, J.5
  • 17
    • 0025909482 scopus 로고
    • Effect of metalloproteinase from Staphylococcus aureus on in vitro stimulation of human lymphocytes
    • Prokesova, L., Porwit-Bobr, Z., Baran, K., Potempa, J., Pospisil, M. & John, C. (1991). Effect of metalloproteinase from Staphylococcus aureus on in vitro stimulation of human lymphocytes. Immunol. Lett. 27, 225-230.
    • (1991) Immunol. Lett. , vol.27 , pp. 225-230
    • Prokesova, L.1    Porwit-Bobr, Z.2    Baran, K.3    Potempa, J.4    Pospisil, M.5    John, C.6
  • 18
    • 0016315138 scopus 로고
    • Substrate specificity of three different extracellular proteolytic enzymes from Staphylococcus aureus
    • Björklind, A. & Jörnvall, H. (1974). Substrate specificity of three different extracellular proteolytic enzymes from Staphylococcus aureus. Biochim. Biophys. Acta 370, 524-529.
    • (1974) Biochim. Biophys. Acta , vol.370 , pp. 524-529
    • Björklind, A.1    Jörnvall, H.2
  • 19
    • 0017164928 scopus 로고
    • Purification et caractérisation d'une protéase extracellulaire de Staphylococcus aureus inhibée par l'E.D.T.A
    • Saheb, S.A. (1976). Purification et caractérisation d'une protéase extracellulaire de Staphylococcus aureus inhibée par l'E.D.T.A. Biochemie 58, 793-804.
    • (1976) Biochemie , vol.58 , pp. 793-804
    • Saheb, S.A.1
  • 20
    • 0015924625 scopus 로고
    • Studies on extracellular proteolytic enzymes from Staphylococcus aureus. II. Isolation and characterization of an EDTA-sensitive protease
    • Arvidson, S.O. (1973). Studies on extracellular proteolytic enzymes from Staphylococcus aureus. II. Isolation and characterization of an EDTA-sensitive protease. Biochim. Biophys Acta 302, 149-157.
    • (1973) Biochim. Biophys Acta , vol.302 , pp. 149-157
    • Arvidson, S.O.1
  • 21
    • 0018082649 scopus 로고
    • Role of a metalloprotease in activation of the precursor of staphylococcal protease
    • Drapeau, G.R. (1978). Role of a metalloprotease in activation of the precursor of staphylococcal protease. J. Bacteriol. 136, 607-613.
    • (1978) J. Bacteriol. , vol.136 , pp. 607-613
    • Drapeau, G.R.1
  • 22
    • 0021680137 scopus 로고
    • Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: A novel class of transition-state analogues for zinc peptidases
    • Monzingo, A.F. & Matthews, B.W. (1984). Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: A novel class of transition-state analogues for zinc peptidases. Biochemistry 23, 5724-5729.
    • (1984) Biochemistry , vol.23 , pp. 5724-5729
    • Monzingo, A.F.1    Matthews, B.W.2
  • 23
    • 0026489329 scopus 로고
    • Structural comparison suggests that thermolysin and related neutral proteases undergo hingebending motion during catalysis
    • Holland, D.R., et al., & Matthews, B.W. (1992). Structural comparison suggests that thermolysin and related neutral proteases undergo hingebending motion during catalysis. Biochemistry 31, 11310-11316.
    • (1992) Biochemistry , vol.31 , pp. 11310-11316
    • Holland, D.R.1    Matthews, B.W.2
  • 24
    • 0026625355 scopus 로고
    • The structure of neutral protease from Bacillus cereus at 0.2-nm resolution
    • Stark, W., Paupitt, R.A., Wilson, K.S. & Jansonius, J.N. (1992). The structure of neutral protease from Bacillus cereus at 0.2-nm resolution. Eur. J. Biochem. 207, 781-791.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 781-791
    • Stark, W.1    Paupitt, R.A.2    Wilson, K.S.3    Jansonius, J.N.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, No. 4. (1994). The CCP4 Suite: Programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 28
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AmoRe: an automated package for molecular replacement Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., McArthur, M.W., Moss, D.S. & Thornton, J. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.4
  • 32
    • 0020462668 scopus 로고
    • Structure of thermolysin refined at 1.6 Å resolution
    • Holmes, M.A. & Matthews, B.W. (1982). Structure of thermolysin refined at 1.6 Å resolution. J. Mol. Biol. 160, 623-639.
    • (1982) J. Mol. Biol. , vol.160 , pp. 623-639
    • Holmes, M.A.1    Matthews, B.W.2
  • 33
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 34
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 35
    • 0000732609 scopus 로고
    • GRASP - Graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP - graphical representation and analysis of surface properties. Biophys. J. 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.