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Volumn 284, Issue 2, 1998, Pages 435-447

Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 Å resolution

Author keywords

Crystal structure; Molecular replacement; Molybdenum; Molybdopterin cofactor; Trimethylamine N oxide reductase

Indexed keywords

MOLYBDENUM; OXIDOREDUCTASE; SOLVENT; TRIMETHYLAMINE OXIDE; TYROSINE;

EID: 0032573427     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2156     Document Type: Article
Times cited : (162)

References (48)
  • 1
    • 0021778428 scopus 로고
    • Bacterial reduction of trimethylamine oxide
    • Barrett E.L., Kwan H.S. Bacterial reduction of trimethylamine oxide. Annu. Rev. Microbiol. 39:1985;131-149
    • (1985) Annu. Rev. Microbiol , vol.39 , pp. 131-149
    • Barrett, E.L.1    Kwan, H.S.2
  • 2
    • 0027412196 scopus 로고
    • ALSCRIPT. a tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT. A tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40
    • (1993) Protein Eng , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 3
    • 0028023353 scopus 로고
    • Multiple states of the molybdenum centre of dimethylsulphoxide reductase from Rhodobacter capsulatus revealed by EPR spectroscopy
    • Bennett B., Benson N., McEwan A.G., Bray R.C. Multiple states of the molybdenum centre of dimethylsulphoxide reductase from Rhodobacter capsulatus revealed by EPR spectroscopy. Eur. J. Biochem. 225:1994;321-331
    • (1994) Eur. J. Biochem , vol.225 , pp. 321-331
    • Bennett, B.1    Benson, N.2    McEwan, A.G.3    Bray, R.C.4
  • 6
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R-value a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 8
    • 0028961901 scopus 로고
    • Structure of the hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan M.K., Mukund S., Kletzin A., Adams M.W.W., Rees D.C. Structure of the hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science. 267:1995;1463-1469
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.W.4    Rees, D.C.5
  • 9
    • 0003154369 scopus 로고
    • Purification and properties of trimethyleamine N-oxide reductase from Shewanella sp. NCMB 400
    • Clarke G.J., Ward F.B. Purification and properties of trimethyleamine N-oxide reductase from Shewanella sp. NCMB 400. J. Gen. Microbiol. 134:1988;379-386
    • (1988) J. Gen. Microbiol , vol.134 , pp. 379-386
    • Clarke, G.J.1    Ward, F.B.2
  • 10
    • 0032573575 scopus 로고    scopus 로고
    • Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from aShewanella species
    • Dos Santos J.P., Iobbi-Nivol C., Couillault C., Giordano G., Mejean V. Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from aShewanella species. J. Mol. Biol. 284:1998;421-433
    • (1998) J. Mol. Biol , vol.284 , pp. 421-433
    • Dos Santos, J.P.1    Iobbi-Nivol, C.2    Couillault, C.3    Giordano, G.4    Mejean, V.5
  • 11
    • 0031447054 scopus 로고    scopus 로고
    • The coordination chemistry and function of the molybdenum centers of the oxomolybdoenzymes
    • Enemark J.H., Garner D.C. The coordination chemistry and function of the molybdenum centers of the oxomolybdoenzymes. J. Biol. Inorg. Chem. 2:1997;817-822
    • (1997) J. Biol. Inorg. Chem , vol.2 , pp. 817-822
    • Enemark, J.H.1    Garner, D.C.2
  • 12
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 13
    • 0030297237 scopus 로고    scopus 로고
    • Microbiological spoilage of fish and fish products
    • Gram L., Huss H.H. Microbiological spoilage of fish and fish products. Int. J. Food Microbiol. 33:1996;121-137
    • (1996) Int. J. Food Microbiol , vol.33 , pp. 121-137
    • Gram, L.1    Huss, H.H.2
  • 14
    • 0031050795 scopus 로고    scopus 로고
    • 70-type sigma factors of group 1 and group 2
    • 70-type sigma factors of group 1 and group 2. J. Bacteriol. 179:1997;1734-1747
    • (1997) J. Bacteriol , vol.179 , pp. 1734-1747
    • Gruber, T.M.1    Bryant, D.A.2
  • 15
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille R. The mononuclear molybdenum enzymes. Chem. Rev. 96:1996;2757-2816
    • (1996) Chem. Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 17
    • 0030014740 scopus 로고    scopus 로고
    • High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli
    • Iobbi-Nivol C., Pommier J., Simala-Grant J., Méjean V., Giordano G. High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli. Biochim. Biophys. Acta. 1294:1996;77-82
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 77-82
    • Iobbi-Nivol, C.1    Pommier, J.2    Simala-Grant, J.3    Méjean, V.4    Giordano, G.5
  • 18
    • 0025228504 scopus 로고
    • Molybdopterin guanine dinucleotide: A modified form of the molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase
    • Johnson J.L., Bastian N.R., Rajagopalan K.V. Molybdopterin guanine dinucleotide a modified form of the molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase. Proc. Natl Acad. Sci. USA. 87:1991;3190-3194
    • (1991) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3190-3194
    • Johnson, J.L.1    Bastian, N.R.2    Rajagopalan, K.V.3
  • 19
    • 0020997912 scopus 로고
    • Dictionary of secondary structures: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of secondary structures pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski R.A., McArthur M.W., Moss D.S., Thronton J.M. PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291
    • (1993) J. Appl. Crystallog , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thronton, J.M.4
  • 22
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati P.V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810
    • (1952) Acta Crystallog , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 23
    • 0031444936 scopus 로고    scopus 로고
    • Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: Crystal structure of the oxidised enzyme at 1.82-Å resolution and the dithionite reduced enzyme at 2.8-Å resolution
    • McAlpine A.S., McEwan A.G., Shaw A.L., Bailey S. Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus crystal structure of the oxidised enzyme at 1.82-Å resolution and the dithionite reduced enzyme at 2.8-Å resolution. J. Biol. Inorg. Chem. 2:1997;690-701
    • (1997) J. Biol. Inorg. Chem , vol.2 , pp. 690-701
    • McAlpine, A.S.1    McEwan, A.G.2    Shaw, A.L.3    Bailey, S.4
  • 24
    • 0032579202 scopus 로고    scopus 로고
    • The high resolution crystal structure of DMSO reductase in complex with DMSO
    • McAlpine A.S., McEwan A.G., Bailey S. The high resolution crystal structure of DMSO reductase in complex with DMSO. J. Mol. Biol. 275:1998;613-623
    • (1998) J. Mol. Biol , vol.275 , pp. 613-623
    • McAlpine, A.S.1    McEwan, A.G.2    Bailey, S.3
  • 25
    • 0000355874 scopus 로고
    • Identification of cytochromes involved in electron transport to trimethylamine N-oxide/dimethylsulfoxide reductase in Rhodobacter capsulatus
    • McEwan A.G., Richardson D.J., Hudig H., Ferguson S.J., Jackson J.B. Identification of cytochromes involved in electron transport to trimethylamine N-oxide/dimethylsulfoxide reductase in Rhodobacter capsulatus. Biochim. Biophys. Acta. 973:1989;308-314
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 308-314
    • McEwan, A.G.1    Richardson, D.J.2    Hudig, H.3    Ferguson, S.J.4    Jackson, J.B.5
  • 28
    • 0004202165 scopus 로고
    • West Lafayette, Indiana: Perdue University
    • Minor W. XDISPLAYF program. 1993;Perdue University, West Lafayette, Indiana
    • (1993) XDISPLAYF Program
    • Minor, W.1
  • 29
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls A., Honig B. A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comp. Chem. 12:1991;435-445
    • (1991) J. Comp. Chem , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 31
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296
    • (1991) Proteins: Struct. Funct. Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 33
    • 0025983512 scopus 로고
    • Novel aspects of the biochemistry of the molybdenum cofactor
    • Rajagopalan K.V. Novel aspects of the biochemistry of the molybdenum cofactor. Advan. Enz. Rel. Areas Mol. Biol. 64:1991;215-290
    • (1991) Advan. Enz. Rel. Areas Mol. Biol , vol.64 , pp. 215-290
    • Rajagopalan, K.V.1
  • 34
    • 0001418372 scopus 로고    scopus 로고
    • The molybdenum cofactors - Perspective from crystal structure
    • Rajagopalan K.V. The molybdenum cofactors - perspective from crystal structure. J. Biol. Inorg. Chem. 2:1997;786-789
    • (1997) J. Biol. Inorg. Chem , vol.2 , pp. 786-789
    • Rajagopalan, K.V.1
  • 35
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • Rajagopalan K.V., Johnson J.L. The pterin molybdenum cofactors. J. Biol. Chem. 267:1992;10199-10202
    • (1992) J. Biol. Chem , vol.267 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 36
    • 0021141418 scopus 로고
    • Amino acid and lactate catabolism in trimethylamine oxide respiration of Alteromonas putrefaciens NCMB 1735
    • Ringo E., Stenberg E., Strom A.R. Amino acid and lactate catabolism in trimethylamine oxide respiration of Alteromonas putrefaciens NCMB 1735. Appl. Environ. Microbiol. 47:1984;1084-1089
    • (1984) Appl. Environ. Microbiol , vol.47 , pp. 1084-1089
    • Ringo, E.1    Stenberg, E.2    Strom, A.R.3
  • 39
    • 0025739201 scopus 로고
    • Differentiation of the multiple S- and N-oxide-reducing activities of Escherichia coli
    • Sambasivarao D., Weiner J.H. Differentiation of the multiple S- and N-oxide-reducing activities of Escherichia coli. Curr. Microbiol. 23:1991;105-110
    • (1991) Curr. Microbiol , vol.23 , pp. 105-110
    • Sambasivarao, D.1    Weiner, J.H.2
  • 40
    • 0023371352 scopus 로고
    • Purification and properties of dimethylsulfoxide reductase containing a molybdenum cofator from photodenitrifier, Rhodopseudomonas sphaeroides f.s. denitrificans
    • Satyoh T., Kurihara F.N. Purification and properties of dimethylsulfoxide reductase containing a molybdenum cofator from photodenitrifier, Rhodopseudomonas sphaeroides f.s. denitrificans. J. Biochem. 102:1987;191-197
    • (1987) J. Biochem , vol.102 , pp. 191-197
    • Satyoh, T.1    Kurihara, F.N.2
  • 41
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin H., Kisker C., Hilton J., Rajagopalan K.V., Rees D.C. Crystal structure of DMSO reductase redox-linked changes in molybdopterin coordination. Science. 272:1996;1615-1621
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 42
    • 0031444023 scopus 로고    scopus 로고
    • The molybdenum-cofactor: A crystallographic perspective
    • Schindelin H., Kisker C., Rees D.C. The molybdenum-cofactor a crystallographic perspective. J. Biol. Inorg. Chem. 2:1997;773-781
    • (1997) J. Biol. Inorg. Chem , vol.2 , pp. 773-781
    • Schindelin, H.1    Kisker, C.2    Rees, D.C.3
  • 43
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution
    • Schneider F., Löwe J., Huber R., Schindelin H., Kisker C., Knablein J. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution. J. Mol. Biol. 263:1996;53-69
    • (1996) J. Mol. Biol , vol.263 , pp. 53-69
    • Schneider, F.1    Löwe, J.2    Huber, R.3    Schindelin, H.4    Kisker, C.5    Knablein, J.6
  • 44
    • 0024388691 scopus 로고
    • The inducible trimethylamine N-oxide reductase of Escherichia coli K12: Biochemical and immunological studies
    • Silvestro A., Pommier J., Giordano G. The inducible trimethylamine N-oxide reductase of Escherichia coli K12 biochemical and immunological studies. Biochim. Biophys. Acta. 999:1989;208-216
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 208-216
    • Silvestro, A.1    Pommier, J.2    Giordano, G.3
  • 45
    • 0029854878 scopus 로고    scopus 로고
    • Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
    • Simala-Grant J.L., Weiner J.H. Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase. Microbiology. 142:1996;3231-3239
    • (1996) Microbiology , vol.142 , pp. 3231-3239
    • Simala-Grant, J.L.1    Weiner, J.H.2
  • 46
    • 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.C., Gibson T.J. CLUSTAL W improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680
    • (1994) Nucl. Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.C.2    Gibson, T.J.3
  • 47
    • 0026800924 scopus 로고
    • Molecular analysis of dimethylsulfoxide reductase: A complex iron-sulfur molybdoenzyme of Escherichia coli
    • Weiner J.H., Rothery R.A., Sambasivarao D., Treiber C.A. Molecular analysis of dimethylsulfoxide reductase a complex iron-sulfur molybdoenzyme of Escherichia coli. Biochim. Biophys. Acta. 1102:1992;1-18
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 1-18
    • Weiner, J.H.1    Rothery, R.A.2    Sambasivarao, D.3    Treiber, C.A.4


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