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Volumn 10, Issue 12, 2002, Pages 1687-1696

Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus

Author keywords

Bacterial; NO; NOS; SANOS; Staphylococcus aureus; Synthase

Indexed keywords

BACTERIAL PROTEIN; ETHYLISOTHIOUREA; NITRIC OXIDE SYNTHASE; OXYGENASE; TETRAHYDROBIOPTERIN; THIOUREA DERIVATIVE; UNCLASSIFIED DRUG; HEME; PRIMER DNA;

EID: 0036899390     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00911-5     Document Type: Article
Times cited : (76)

References (40)
  • 1
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • Knowles R.G., Moncada S. Nitric oxide synthases in mammals. Biochem. J. 298:1994;249-258.
    • (1994) Biochem. J. , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 2
    • 0012008697 scopus 로고    scopus 로고
    • Biochemistry of nitric oxide
    • Cooper C.E. Biochemistry of nitric oxide. Biochim. Biophys. Acta. 1411:1999;215-216.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 215-216
    • Cooper, C.E.1
  • 4
    • 0028276990 scopus 로고
    • Evidence for a bidomain structure of constitutive cerebellar nitric oxide synthase
    • Sheta E.A., McMillan K., Masters B.S. Evidence for a bidomain structure of constitutive cerebellar nitric oxide synthase. J. Biol. Chem. 269:1994;15147-15153.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15147-15153
    • Sheta, E.A.1    McMillan, K.2    Masters, B.S.3
  • 5
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains
    • Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E., Santillano D.R., Wu Z., Huang F., Xia H., Peters M.F.et al. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains. Cell. 84:1996;757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5    Santillano, D.R.6    Wu, Z.7    Huang, F.8    Xia, H.9    Peters, M.F.10
  • 6
    • 0031055372 scopus 로고    scopus 로고
    • Evidence for PDZ domains in bacteria, yeast, and plants
    • Ponting C.P. Evidence for PDZ domains in bacteria, yeast, and plants. Protein Sci. 6:1997;464-468.
    • (1997) Protein Sci. , vol.6 , pp. 464-468
    • Ponting, C.P.1
  • 7
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • Alderton W.K., Cooper C.E., Knowles R.G. Nitric oxide synthases. structure, function and inhibition Biochem. J. 357:2001;593-615.
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 9
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • Raman C.S., Li H., Martasek P., Kral V., Masters B.S., Poulos T.L. Crystal structure of constitutive endothelial nitric oxide synthase. a paradigm for pterin function involving a novel metal center Cell. 95:1998;939-950.
    • (1998) Cell , vol.95 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Kral, V.4    Masters, B.S.5    Poulos, T.L.6
  • 12
    • 0033597930 scopus 로고    scopus 로고
    • Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase
    • Li H., Raman C.S., Glaser C.B., Blasko E., Young T.A., Parkinson J.F., Whitlow M., Poulos T.L. Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. J. Biol. Chem. 274:1999;21276-21284.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21276-21284
    • Li, H.1    Raman, C.S.2    Glaser, C.B.3    Blasko, E.4    Young, T.A.5    Parkinson, J.F.6    Whitlow, M.7    Poulos, T.L.8
  • 13
    • 0035813091 scopus 로고    scopus 로고
    • Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase
    • Zhang J., Martasek P., Paschke R., Shea T., Siler Masters B.S., Kim J.J. Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase. J. Biol. Chem. 276:2001;37506-37513.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37506-37513
    • Zhang, J.1    Martasek, P.2    Paschke, R.3    Shea, T.4    Siler Masters, B.S.5    Kim, J.J.6
  • 14
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S., Kim J.J. Three-dimensional structure of NADPH-cytochrome P450 reductase. prototype for FMN- and FAD-containing enzymes Proc. Natl. Acad. Sci. USA. 94:1997;8411-8416.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.5    Kim, J.J.6
  • 15
    • 0032923887 scopus 로고    scopus 로고
    • Bacterial nitric oxide synthesis
    • Cutruzzola F. Bacterial nitric oxide synthesis. Biochim. Biophys. Acta. 1411:1999;231-249.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 231-249
    • Cutruzzola, F.1
  • 16
    • 0025287522 scopus 로고
    • Steady-state nitric oxide concentrations during denitrification
    • Goretski J., Zafiriou O.C., Hollocher T.C. Steady-state nitric oxide concentrations during denitrification. J. Biol. Chem. 265:1990;11535-11538.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11535-11538
    • Goretski, J.1    Zafiriou, O.C.2    Hollocher, T.C.3
  • 17
    • 0028960382 scopus 로고
    • Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages
    • Nunoshiba T., DeRojas-Walker T., Tannenbaum S.R., Demple B. Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages. Infect. Immun. 63:1995;794-798.
    • (1995) Infect. Immun. , vol.63 , pp. 794-798
    • Nunoshiba, T.1    DeRojas-Walker, T.2    Tannenbaum, S.R.3    Demple, B.4
  • 18
    • 0029831326 scopus 로고    scopus 로고
    • Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12
    • Poole R.K., Anjum M.F., Membrillo-Hernandez J., Kim S.O., Hughes M.N., Stewart V. Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12. J. Bacteriol. 178:1996;5487-5492.
    • (1996) J. Bacteriol. , vol.178 , pp. 5487-5492
    • Poole, R.K.1    Anjum, M.F.2    Membrillo-Hernandez, J.3    Kim, S.O.4    Hughes, M.N.5    Stewart, V.6
  • 19
    • 0028048809 scopus 로고
    • A bacterial nitric oxide synthase from a Nocardia species
    • Chen Y., Rosazza J.P. A bacterial nitric oxide synthase from a Nocardia species. Biochem. Biophys. Res. Commun. 203:1994;1251-1258.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1251-1258
    • Chen, Y.1    Rosazza, J.P.2
  • 20
    • 0029154131 scopus 로고
    • Purification and characterization of nitric oxide synthase (NOSNoc) from a Nocardia species
    • Chen Y., Rosazza J.P. Purification and characterization of nitric oxide synthase (NOSNoc) from a Nocardia species. J. Bacteriol. 177:1995;5122-5128.
    • (1995) J. Bacteriol. , vol.177 , pp. 5122-5128
    • Chen, Y.1    Rosazza, J.P.2
  • 23
    • 0000872980 scopus 로고    scopus 로고
    • Structural themes determining function in nitric oxide synthases
    • K.M. Kadish, K.M. Smith, R. Guilard, & Volume 4. London: Academic Press
    • Raman C.S., Martasek P., Masters B.S.S. Structural themes determining function in nitric oxide synthases. Kadish K.M., Smith K.M., Guilard R., Volume 4 The Porphyrin Handbook. 2000;Academic Press, London.
    • (2000) The Porphyrin Handbook
    • Raman, C.S.1    Martasek, P.2    Masters, B.S.S.3
  • 25
    • 0037013239 scopus 로고    scopus 로고
    • Direct evidence for nitric oxide production by a nitric oxide synthase-like protein from Bacillus subtilis
    • Adak S., Aulak K.S., Stuehr D.J. Direct evidence for nitric oxide production by a nitric oxide synthase-like protein from Bacillus subtilis. J. Biol. Chem. 277:2002;16167-16171.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16167-16171
    • Adak, S.1    Aulak, K.S.2    Stuehr, D.J.3
  • 27
    • 0028848093 scopus 로고
    • Cysteine 99 of endothelial nitric oxide synthase (NOS-III) is critical for tetrahydrobiopterin-dependent NOS-III stability and activity
    • Chen P.F., Tsai A.L., Wu K.K. Cysteine 99 of endothelial nitric oxide synthase (NOS-III) is critical for tetrahydrobiopterin-dependent NOS-III stability and activity. Biochem. Biophys. Res. Commun. 215:1995;1119-1129.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 1119-1129
    • Chen, P.F.1    Tsai, A.L.2    Wu, K.K.3
  • 28
    • 0030758321 scopus 로고    scopus 로고
    • Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction
    • Ghosh D.K., Wu C., Pitters E., Moloney M., Werner E.R., Mayer B., Stuehr D.J. Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction. Biochemistry. 36:1997;10609-10619.
    • (1997) Biochemistry , vol.36 , pp. 10609-10619
    • Ghosh, D.K.1    Wu, C.2    Pitters, E.3    Moloney, M.4    Werner, E.R.5    Mayer, B.6    Stuehr, D.J.7
  • 29
    • 0040943986 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase: Modulations of the distal heme site produced by progressive N-terminal deletions
    • Rodriguez-Crespo I., Moenne-Loccoz P., Loehr T.M., Ortiz de Montellano P.R. Endothelial nitric oxide synthase. modulations of the distal heme site produced by progressive N-terminal deletions Biochemistry. 36:1997;8530-8538.
    • (1997) Biochemistry , vol.36 , pp. 8530-8538
    • Rodriguez-Crespo, I.1    Moenne-Loccoz, P.2    Loehr, T.M.3    Ortiz de Montellano, P.R.4
  • 31
    • 0033571213 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase: Role of the N-terminal β-hairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction
    • Ghosh D.K., Crane B.R., Ghosh S., Wolan D., Gachhui R., Crooks C., Presta A., Tainer J.A., Getzoff E.D., Stuehr D.J. Inducible nitric oxide synthase. role of the N-terminal β-hairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction EMBO J. 18:1999;6260-6270.
    • (1999) EMBO J. , vol.18 , pp. 6260-6270
    • Ghosh, D.K.1    Crane, B.R.2    Ghosh, S.3    Wolan, D.4    Gachhui, R.5    Crooks, C.6    Presta, A.7    Tainer, J.A.8    Getzoff, E.D.9    Stuehr, D.J.10
  • 33
    • 0028848015 scopus 로고
    • Isothioureas: Potent inhibitors of nitric oxide synthases with variable isoform selectivity
    • Southan G.J., Szabo C., Thiemermann C. Isothioureas. potent inhibitors of nitric oxide synthases with variable isoform selectivity Br. J. Pharmacol. 114:1995;510-516.
    • (1995) Br. J. Pharmacol. , vol.114 , pp. 510-516
    • Southan, G.J.1    Szabo, C.2    Thiemermann, C.3
  • 34
    • 0028898303 scopus 로고
    • Hydrogen peroxide-supported oxidation of NG-hydroxy-L-arginine by nitric oxide synthase
    • Pufahl R.A., Wishnok J.S., Marletta M.A. Hydrogen peroxide-supported oxidation of NG-hydroxy-L-arginine by nitric oxide synthase. Biochemistry. 34:1995;1930-1941.
    • (1995) Biochemistry , vol.34 , pp. 1930-1941
    • Pufahl, R.A.1    Wishnok, J.S.2    Marletta, M.A.3
  • 36
    • 0034721839 scopus 로고    scopus 로고
    • Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism
    • Adak S., Wang Q., Stuehr D.J. Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism. J. Biol. Chem. 275:2000;33554-33561.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33554-33561
    • Adak, S.1    Wang, Q.2    Stuehr, D.J.3
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in the oscillation mode
    • C.W. Carter, & R.M. Sweet. London: Academic Press. 307-326.pp
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in the oscillation mode. Carter C.W., Sweet R.M. Methods in Enzymology. 1996;Academic Press, London. 307-326.pp.
    • (1996) Methods in Enzymology
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0037125928 scopus 로고    scopus 로고
    • Structure of a nitric oxide synthase heme protein from Bacillus subtilis
    • Pant K., Bilwes A.M., Adak S., Stuehr D.J., Crane B.R. Structure of a nitric oxide synthase heme protein from Bacillus subtilis. Biochemistry. 41:2002;11071-11079.
    • (2002) Biochemistry , vol.41 , pp. 11071-11079
    • Pant, K.1    Bilwes, A.M.2    Adak, S.3    Stuehr, D.J.4    Crane, B.R.5
  • 40
    • 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 J.D., Higgins D.G., Gibson T.J. Clustal w. improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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