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Volumn 10, Issue 9, 2002, Pages 1261-1272

Gene sequence and the 1.8 Å crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas

Author keywords

Formate dehydrogenase; Iron sulfur cluster; Molybdopterin; Selenium; Selenocysteine; Tungsten

Indexed keywords

AMINO ACID; CARBON DIOXIDE; FORMATE DEHYDROGENASE; NITRATE REDUCTASE; PROTON; TUNGSTEN; WATER; PROTEIN SUBUNIT;

EID: 0036711479     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00826-2     Document Type: Article
Times cited : (157)

References (39)
  • 2
    • 0034852815 scopus 로고    scopus 로고
    • Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: Metal identification and preliminary structural data by multi-wavelength crystallography
    • Raaijmakers H., Teixeira S., Dias J.M., Almendra M.J., Brondino C.D., Moura I., Moura J.J.G., Romão M.J. Tungsten-containing formate dehydrogenase from Desulfovibrio gigas. metal identification and preliminary structural data by multi-wavelength crystallography J. Biol. Inorg. Chem. 6:2001;398-404.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 398-404
    • Raaijmakers, H.1    Teixeira, S.2    Dias, J.M.3    Almendra, M.J.4    Brondino, C.D.5    Moura, I.6    Moura, J.J.G.7    Romão, M.J.8
  • 3
    • 0028787109 scopus 로고
    • Purification and characterization of the formate dehydrogenase from Desulfovibrio vulgaris Hildenborough
    • Sebban C., Blanchard L., Bruschi M., Guerslequin F. Purification and characterization of the formate dehydrogenase from Desulfovibrio vulgaris Hildenborough. FEMS Microbiol. Lett. 133:1995;143-149.
    • (1995) FEMS Microbiol. Lett. , vol.133 , pp. 143-149
    • Sebban, C.1    Blanchard, L.2    Bruschi, M.3    Guerslequin, F.4
  • 4
    • 0030900976 scopus 로고    scopus 로고
    • Formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774: Isolation and spectroscopic characterization of the active sites (heme, iron-sulfur centres and molybdenum)
    • Costa C., Teixeira M., LeGall J., Moura J.J.G., Moura I. Formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774. isolation and spectroscopic characterization of the active sites (heme, iron-sulfur centres and molybdenum) J. Biol. Inorg. Chem. 2:1997;198-208.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 198-208
    • Costa, C.1    Teixeira, M.2    LeGall, J.3    Moura, J.J.G.4    Moura, I.5
  • 7
    • 0002155983 scopus 로고    scopus 로고
    • Structure and function of the xanthine-oxidase family of molybdenum enzymes
    • H.A.O. Hill, A.J. Sadler, & A.J. Thomson. Berlin: Springer-Verlag 69-96pp
    • Romão M.J., Huber R. Structure and function of the xanthine-oxidase family of molybdenum enzymes. Hill H.A.O., Sadler A.J., Thomson A.J. In Metal Sites in Proteins and Models - Redox Centers, Structure and Bonding. 1998;Springer-Verlag, Berlin. 69-96pp.
    • (1998) In Metal Sites in Proteins and Models - Redox Centers, Structure and Bonding
    • Romão, M.J.1    Huber, R.2
  • 8
    • 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
  • 9
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor containing enzymes: Structure and mechanism
    • Kisker C., Schindelin H., Rees D.C. Molybdenum-cofactor containing enzymes. structure and mechanism Annu. Rev. Biochem. 66:1997;233-267.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 10
    • 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., Knäblein 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    Knäblein, J.6
  • 11
    • 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
  • 13
    • 0031043109 scopus 로고    scopus 로고
    • Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine, and a [4Fe-4S] cluster
    • Boyington J.C., Gladyshev V.N., Khangulov S.V., Stadtman T.C., Sun P.D. Crystal structure of formate dehydrogenase H. catalysis involving Mo, molybdopterin, selenocysteine, and a [4Fe-4S] cluster Science. 275:1997;1305-1308.
    • (1997) Science , vol.275 , pp. 1305-1308
    • Boyington, J.C.1    Gladyshev, V.N.2    Khangulov, S.V.3    Stadtman, T.C.4    Sun, P.D.5
  • 14
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks B. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:1996;393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.1
  • 15
    • 0033532176 scopus 로고    scopus 로고
    • Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat Pathway
    • Rodrigue A., Chanal A., Beck K., Müller M., Wu L.-F. Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat Pathway. J. Biol. Chem. 274:1999;13223-13228.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Müller, M.4    Wu, L.-F.5
  • 16
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R.J., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:1999;458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.J.2    Lamzin, V.S.3
  • 18
    • 0032502268 scopus 로고    scopus 로고
    • Selenium-containing formate dehydrogenase H from Escherichia coli: A molybdopterin enzyme that catalyses formate oxidation without oxygen transfer
    • Khangulov S.V., Gladyshev V.N., Dismukes G.C., Stadtman T.C. Selenium-containing formate dehydrogenase H from Escherichia coli. a molybdopterin enzyme that catalyses formate oxidation without oxygen transfer Biochemistry. 37:1998;3518-3528.
    • (1998) Biochemistry , vol.37 , pp. 3518-3528
    • Khangulov, S.V.1    Gladyshev, V.N.2    Dismukes, G.C.3    Stadtman, T.C.4
  • 20
    • 0029786946 scopus 로고    scopus 로고
    • Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: Evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins
    • Moulis J.M., Sieker L.C., Wilson K.S., Dauter Z. Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum. evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins Protein Sci. 5:1996;1765-1775.
    • (1996) Protein Sci. , vol.5 , pp. 1765-1775
    • Moulis, J.M.1    Sieker, L.C.2    Wilson, K.S.3    Dauter, Z.4
  • 21
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Nicolet Y., Piras C., Legrand P., Hatchikian E.C., Fontecilla-Camps J.C. Desulfovibrio desulfuricans iron hydrogenase. the structure shows unusual coordination to an active site Fe binuclear center Structure. 7:1999;13-23.
    • (1999) Structure , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, E.C.4    Fontecilla-Camps, J.C.5
  • 22
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka M., Törnroth S., Byrne B., Iwata S. Molecular basis of proton motive force generation. structure of formate dehydrogenase-N Science. 295:2002;1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Törnroth, S.2    Byrne, B.3    Iwata, S.4
  • 23
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
    • Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase. structure-based mechanism of conversion Proc. Natl. Acad. Sci. USA. 97:2000;10723-10728.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Nishino, T.5    Pai, E.F.6
  • 24
    • 0035816594 scopus 로고    scopus 로고
    • Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum
    • Makdessi K., Andreesen J.R., Pich A. Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. J. Biol. Chem. 276:2001;24557-24564.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24557-24564
    • Makdessi, K.1    Andreesen, J.R.2    Pich, A.3
  • 27
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman H., Gerber A.S., Hartl D.L. Genetic applications of an inverse polymerase chain reaction. Genetics. 120:1988;621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 28
    • 0023787609 scopus 로고
    • A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences
    • Triglia T., Peterson M.G., Kemp D.J. A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences. Nucleic Acids Res. 16:1988;8186.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 8186
    • Triglia, T.1    Peterson, M.G.2    Kemp, D.J.3
  • 29
    • 0024584243 scopus 로고
    • Novel use of the polymerase chain reaction to amplify cellular DNA adjacent to an integrated provirus
    • Silver J., Keerikatte V. Novel use of the polymerase chain reaction to amplify cellular DNA adjacent to an integrated provirus. J. Virol. 63:1989;1924-1928.
    • (1989) J. Virol. , vol.63 , pp. 1924-1928
    • Silver, J.1    Keerikatte, V.2
  • 30
    • 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
  • 32
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 The CCP4 suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 37
    • 0002908272 scopus 로고
    • TURBO-FRODO, molecular modeling package
    • Mountain View, CA: Silicon Graphics
    • Roussel, A., and Cambilau, C. (1989). TURBO-FRODO, molecular modeling package. In Silicon Graphics Geometry Partner Directory, (Mountain View, CA: Silicon Graphics), pp. 77-78.
    • (1989) Silicon Graphics Geometry Partner Directory , pp. 77-78
    • Roussel, A.1    Cambilau, C.2
  • 38
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;134-138.
    • (1991) Proteins , vol.11 , pp. 134-138
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 39
    • 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


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