메뉴 건너뛰기




Volumn 77, Issue 5, 2010, Pages 1172-1185

Biological and structural characterization of the Mycobacterium smegmatis nitroreductase NfnB, and its role in benzothiazinone resistance

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMYCOBACTERIAL AGENT; BENZOTHIAZINONE; BTZ 043; BTZ 045; NITROREDUCTASE; NITROREDUCTASE NFNB; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UNCLASSIFIED DRUG;

EID: 77956163145     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07277.x     Document Type: Article
Times cited : (68)

References (40)
  • 2
    • 29144482496 scopus 로고    scopus 로고
    • Comprehensive identification of "druggable" protein ligand binding sites
    • An, J., Totrov, M. Abagyan, R. (2004) Comprehensive identification of "druggable" protein ligand binding sites. Genome Inform 15 : 31 41.
    • (2004) Genome Inform , vol.15 , pp. 31-41
    • An, J.1    Totrov, M.2    Abagyan, R.3
  • 3
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by directed evolution
    • van den Berg, S., Lofdahl, P.A., Hard, T. Berglund, H. (2006) Improved solubility of TEV protease by directed evolution. J Biotechnol 121 : 291 298.
    • (2006) J Biotechnol , vol.121 , pp. 291-298
    • Van Den Berg, S.1    Lofdahl, P.A.2    Hard, T.3    Berglund, H.4
  • 4
  • 6
    • 73649143180 scopus 로고    scopus 로고
    • High content screening identifies decaprenyl-phosphoribose 2′ epimerase as a target for intracellular antimycobacterial inhibitors
    • Christophe, T., Jackson, M., Jeon, H.K., Fenistein, D., Contreras-Dominguez, M., Kim, J., et al. (2009) High content screening identifies decaprenyl-phosphoribose 2′ epimerase as a target for intracellular antimycobacterial inhibitors. PLoS Pathog 5 : e10000645.
    • (2009) PLoS Pathog , vol.5 , pp. 10000645
    • Christophe, T.1    Jackson, M.2    Jeon, H.K.3    Fenistein, D.4    Contreras-Dominguez, M.5    Kim, J.6
  • 7
    • 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 50 : 760 763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 8
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I.W., Leaver-Fay, A., Chen, V.B., Block, J.N., Kapral, G.J., Wang, X., et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35 : W375 W383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5    Wang, X.6
  • 9
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T.J., Nielsen, J.E., McCammon, J.A. Baker, N.A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 32 : W665 W667.
    • (2004) Nucleic Acids Res , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 10
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta crystallogr D 60 : 2126 2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 11
    • 0037192818 scopus 로고    scopus 로고
    • Structures of nitroreductase in three states. Effects of inhibitor binding and reduction
    • Haynes, C.A., Koder, R.L., Miller, A.F. Rodgers, D.W. (2002) Structures of nitroreductase in three states. Effects of inhibitor binding and reduction. J Biol Chem 277 : 11513 11520.
    • (2002) J Biol Chem , vol.277 , pp. 11513-11520
    • Haynes, C.A.1    Koder, R.L.2    Miller, A.F.3    Rodgers, D.W.4
  • 12
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm, L., Kaariainen, S., Rosenstrom, P. Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24 : 2780 2781.
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 13
    • 0141790765 scopus 로고    scopus 로고
    • Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form
    • Johansson, E., Parkinson, G.N., Denny, W.A. Neidle, S. (2003) Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form. J Med Chem 46 : 4009 4020.
    • (2003) J Med Chem , vol.46 , pp. 4009-4020
    • Johansson, E.1    Parkinson, G.N.2    Denny, W.A.3    Neidle, S.4
  • 14
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26 : 795 800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 15
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E. Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D 60 : 2256 2268.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 16
    • 67349129059 scopus 로고    scopus 로고
    • Characterization of Escherichia coli nitroreductase NfsB in the metabolism of nitrobenzodiazepines
    • Linwu, S.W., Syu, C.J., Chen, Y.L., Wang, A.H. Peng, F.C. (2009) Characterization of Escherichia coli nitroreductase NfsB in the metabolism of nitrobenzodiazepines. Biochem Pharmacol 78 : 96 103.
    • (2009) Biochem Pharmacol , vol.78 , pp. 96-103
    • Linwu, S.W.1    Syu, C.J.2    Chen, Y.L.3    Wang, A.H.4    Peng, F.C.5
  • 17
    • 0035946957 scopus 로고    scopus 로고
    • The structure of Escherichia coli nitroreductase complexed with nicotinic acid: Three crystal forms at 1.7 Å, 1.8 Å and 2.4 Å resolution
    • Lovering, A.L., Hyde, E.I., Searle, P.F. White, S.A. (2001) The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 Å, 1.8 Å and 2.4 Å resolution. J Mol Biol 309 : 203 213.
    • (2001) J Mol Biol , vol.309 , pp. 203-213
    • Lovering, A.L.1    Hyde, E.I.2    Searle, P.F.3    White, S.A.4
  • 18
  • 19
    • 65649096556 scopus 로고    scopus 로고
    • Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis
    • Makarov, V., Manina, G., Mikusova, K., Möllmann, U., Ryabova, O., Saint-Joanis, B., et al. (2009) Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis. Science 324 : 801 804.
    • (2009) Science , vol.324 , pp. 801-804
    • Makarov, V.1    Manina, G.2    Mikusova, K.3    Möllmann, U.4    Ryabova, O.5    Saint-Joanis, B.6
  • 20
    • 31044452898 scopus 로고    scopus 로고
    • Identification of a nitroimidazo-oxazine-specific protein involved in PA-824 resistance in Mycobacterium tuberculosis
    • Manjunatha, U.H., Boshoff, H., Dowd, C.S., Zhang, L., Albert, T.J., Norton, J.E., et al. (2006) Identification of a nitroimidazo-oxazine-specific protein involved in PA-824 resistance in Mycobacterium tuberculosis. Proc Natl Acad Sci USA 103 : 431 436.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 431-436
    • Manjunatha, U.H.1    Boshoff, H.2    Dowd, C.S.3    Zhang, L.4    Albert, T.J.5    Norton, J.E.6
  • 21
    • 0031569863 scopus 로고    scopus 로고
    • Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis
    • Marcinkeviciene, J. Blanchard, J.S. (1997) Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis. Arch Biochem Biophys 340 : 168 176.
    • (1997) Arch Biochem Biophys , vol.340 , pp. 168-176
    • Marcinkeviciene, J.1    Blanchard, J.S.2
  • 23
    • 28044470257 scopus 로고    scopus 로고
    • Decaprenylphosphoryl arabinofuranose, the donor of the d-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose
    • Mikusova, K., Huang, H., Yagi, T., Holsters, M., Vereecke, D., D'Haeze, W., et al. (2005) Decaprenylphosphoryl arabinofuranose, the donor of the d-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose. J Bacteriol 187 : 8020 8025.
    • (2005) J Bacteriol , vol.187 , pp. 8020-8025
    • Mikusova, K.1    Huang, H.2    Yagi, T.3    Holsters, M.4    Vereecke, D.5    D'Haeze, W.6
  • 24
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J. Merritt, E.A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D 62 : 439 450.
    • (2006) Acta Crystallogr D , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 25
    • 0033880508 scopus 로고    scopus 로고
    • Use of a flexible cassette method to generate a double unmarked Mycobacterium tuberculosis tlyA plcABC mutant by gene replacement
    • Parish, T. Stoker, N.G. (2000) Use of a flexible cassette method to generate a double unmarked Mycobacterium tuberculosis tlyA plcABC mutant by gene replacement. Microbiology 146 : 1969 1975.
    • (2000) Microbiology , vol.146 , pp. 1969-1975
    • Parish, T.1    Stoker, N.G.2
  • 26
    • 0034609776 scopus 로고    scopus 로고
    • Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: A prodrug-activating enzyme
    • Parkinson, G.N., Skelly, J.V. Neidle, S. (2000) Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme. J Med Chem 43 : 3624 3631.
    • (2000) J Med Chem , vol.43 , pp. 3624-3631
    • Parkinson, G.N.1    Skelly, J.V.2    Neidle, S.3
  • 27
    • 77950141431 scopus 로고    scopus 로고
    • Clinical isolates of Mycobacterium tuberculosis in four european hospitals are uniformly susceptible to benzothiazinones
    • Pasca, M.R., Degiacomi, G., De Jesus Lopes Ribeiro, A.L., Zara, F., De Mori, P., Heym, B., et al. (2010) Clinical isolates of Mycobacterium tuberculosis in four european hospitals are uniformly susceptible to benzothiazinones. Antimicrob Agents Chemother 54 : 1616 1618.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1616-1618
    • Pasca, M.R.1    Degiacomi, G.2    De Jesus Lopes Ribeiro, A.L.3    Zara, F.4    De Mori, P.5    Heym, B.6
  • 28
    • 0036175346 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis putative classical nitroreductase gene whose expression is coregulated with that of the acr gene within macrophages, in standing versus shaking cultures, and under low oxygen conditions
    • Purkayastha, A., McCue, L.A. McDonough, K.A. (2002) Identification of a Mycobacterium tuberculosis putative classical nitroreductase gene whose expression is coregulated with that of the acr gene within macrophages, in standing versus shaking cultures, and under low oxygen conditions. Infect Immun 70 : 1518 1529.
    • (2002) Infect Immun , vol.70 , pp. 1518-1529
    • Purkayastha, A.1    McCue, L.A.2    McDonough, K.A.3
  • 29
    • 17144417314 scopus 로고    scopus 로고
    • Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme
    • Race, P.R., Lovering, A.L., Green, R.M., Ossor, A., White, S.A., Searle, P.F., et al. (2005) Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme. J Biol Chem 280 : 13256 13264.
    • (2005) J Biol Chem , vol.280 , pp. 13256-13264
    • Race, P.R.1    Lovering, A.L.2    Green, R.M.3    Ossor, A.4    White, S.A.5    Searle, P.F.6
  • 30
    • 67149118143 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis: Drug resistance and future perspectives
    • Riccardi, G., Pasca, M.R. Buroni, S. (2009) Mycobacterium tuberculosis: drug resistance and future perspectives. Future Microbiol 4 : 597 614.
    • (2009) Future Microbiol , vol.4 , pp. 597-614
    • Riccardi, G.1    Pasca, M.R.2    Buroni, S.3
  • 32
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti, C.M., Boyd, D.H. Rubin, E.J. (2003) Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48 : 77 84.
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 33
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G.M. (2008) A short history of SHELX. Acta Crystallogr A 64 : 112 122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 34
    • 57149099588 scopus 로고    scopus 로고
    • PA-824 kills nonreplicating Mycobacterium tuberculosis by intracellular NO release
    • Singh, R., Manjunatha, U., Boshoff, H.I., Ha, Y.H., Niyomrattanakit, P., Ledwidge, R., et al. (2008) PA-824 kills nonreplicating Mycobacterium tuberculosis by intracellular NO release. Science 322 : 1392 1395.
    • (2008) Science , vol.322 , pp. 1392-1395
    • Singh, R.1    Manjunatha, U.2    Boshoff, H.I.3    Ha, Y.H.4    Niyomrattanakit, P.5    Ledwidge, R.6
  • 35
    • 0034702247 scopus 로고    scopus 로고
    • A small-molecule nitroimidazopyran drug candidate for the treatment of tuberculosis
    • Stover, C.K., Warrener, P., VanDevanter, D.R., Sherman, D.R., Arain, T.M., Langhorne, M.H., et al. (2000) A small-molecule nitroimidazopyran drug candidate for the treatment of tuberculosis. Nature 405 : 962 966.
    • (2000) Nature , vol.405 , pp. 962-966
    • Stover, C.K.1    Warrener, P.2    Vandevanter, D.R.3    Sherman, D.R.4    Arain, T.M.5    Langhorne, M.H.6
  • 36
    • 34548851418 scopus 로고    scopus 로고
    • Hepatic nitroreduction, toxicity and toxicokinetics of the anti-tumour prodrug CB 1954 in mouse and rat
    • Tang, M.H., Helsby, N.A., Goldthorpe, M.A., Thompson, K.M., Al-Ali, S. Tingle, M.D. (2007) Hepatic nitroreduction, toxicity and toxicokinetics of the anti-tumour prodrug CB 1954 in mouse and rat. Toxicology 240 : 70 85.
    • (2007) Toxicology , vol.240 , pp. 70-85
    • Tang, M.H.1    Helsby, N.A.2    Goldthorpe, M.A.3    Thompson, K.M.4    Al-Ali, S.5    Tingle, M.D.6
  • 37
    • 0031302358 scopus 로고    scopus 로고
    • Flexible protein-ligand docking by global energy optimization in internal coordinates
    • Totrov, M. Abagyan, R. (1997) Flexible protein-ligand docking by global energy optimization in internal coordinates. Proteins 29 (Suppl. 1 215 220.
    • (1997) Proteins , vol.29 , Issue.SUPPL. 1 , pp. 215-220
    • Totrov, M.1    Abagyan, R.2
  • 39
    • 43549101762 scopus 로고    scopus 로고
    • Biosynthesis of d-arabinose in mycobacteria - A novel bacterial pathway with implications for antimycobacterial therapy
    • Wolucka, B.A. (2008) Biosynthesis of d-arabinose in mycobacteria - a novel bacterial pathway with implications for antimycobacterial therapy. FEBS J 68 : 2602 2613.
    • (2008) FEBS J , vol.68 , pp. 2602-2613
    • Wolucka, B.A.1
  • 40
    • 0029745672 scopus 로고    scopus 로고
    • Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase
    • Zenno, S., Koike, H., Kumar, A.N., Jayaraman, R., Tanokura, M. Saigo, K. (1996) Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. J Bacteriol 178 : 4508 4514.
    • (1996) J Bacteriol , vol.178 , pp. 4508-4514
    • Zenno, S.1    Koike, H.2    Kumar, A.N.3    Jayaraman, R.4    Tanokura, M.5    Saigo, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.