메뉴 건너뛰기




Volumn 463, Issue 7280, 2010, Pages 507-512

Structure of a bacterial homologue of vitamin K epoxide reductase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; METHIONINE; QUINONE DERIVATIVE; THIOREDOXIN; UNCLASSIFIED DRUG; VITAMIN K EPOXIDE REDUCTASE; VITAMIN K GROUP; WARFARIN;

EID: 75749153714     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08720     Document Type: Article
Times cited : (165)

References (43)
  • 2
    • 40949129912 scopus 로고    scopus 로고
    • Structure and function of vitamin K epoxide reductase
    • Tie, J. K. & Stafford, D. W. Structure and function of vitamin K epoxide reductase. Vitam. Horm. 78, 103-130 (2008).
    • (2008) Vitam. Horm. , vol.78 , pp. 103-130
    • Tie, J.K.1    Stafford, D.W.2
  • 3
    • 0017620768 scopus 로고
    • Vitamin K-dependent formation of c-carboxyglutamic acid
    • Stenflo, J. & Suttie, J. W. Vitamin K-dependent formation of c-carboxyglutamic acid. Annu. Rev. Biochem. 46, 157-172 (1977).
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 157-172
    • Stenflo, J.1    Suttie, J.W.2
  • 4
    • 0033559305 scopus 로고    scopus 로고
    • Vitamin K-dependent biosynthesis of c-carboxyglutamic acid
    • Furie, B., Bouchard, B. A. & Furie, B. C. Vitamin K-dependent biosynthesis of c-carboxyglutamic acid. Blood 93, 1798-1808 (1999).
    • (1999) Blood , vol.93 , pp. 1798-1808
    • Furie, B.1    Bouchard, B.A.2    Furie, B.C.3
  • 5
    • 34047258016 scopus 로고    scopus 로고
    • Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction
    • Wajih, N., Hutson, S. M. & Wallin, R. Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction. J. Biol. Chem. 282, 2626-2635 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 2626-2635
    • Wajih, N.1    Hutson, S.M.2    Wallin, R.3
  • 6
    • 0026547487 scopus 로고
    • Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase
    • Soute, B. A., Groenen-van Dooren, M. M., Holmgren, A., Lundstrom, J. & Vermeer, C. Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase. Biochem. J. 281, 255-259 (1992).
    • (1992) Biochem. J. , vol.281 , pp. 255-259
    • Soute, B.A.1    Groenen-Van Dooren, M.M.2    Holmgren, A.3    Lundstrom, J.4    Vermeer, C.5
  • 7
    • 33845878853 scopus 로고    scopus 로고
    • Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2
    • Chu, P. H., Huang, T. Y., Williams, J. & Stafford, D. W. Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2. Proc. Natl Acad. Sci. USA 103, 19308-19313 (2006)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 19308-19313
    • Chu, P.H.1    Huang, T.Y.2    Williams, J.3    Stafford, D.W.4
  • 8
    • 60849097257 scopus 로고    scopus 로고
    • Estimationof thewarfarin dose with clinical and pharmacogenetic data
    • The International Warfarin Pharmacogenetics Consortium
    • The International Warfarin Pharmacogenetics Consortium. Estimationof thewarfarin dose with clinical and pharmacogenetic data. N. Engl. J. Med. 360, 753-764 (2009).
    • (2009) N. Engl. J. Med. , vol.360 , pp. 753-764
  • 9
    • 10744228888 scopus 로고    scopus 로고
    • Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2
    • Rost, S. et al. Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2. Nature 427, 537-541 (2004).
    • (2004) Nature , vol.427 , pp. 537-541
    • Rost, S.1
  • 10
    • 3242786500 scopus 로고    scopus 로고
    • Vitamin K epoxide reductase: Homology, active site and catalytic mechanism
    • Goodstadt, L. & Ponting, C. P. Vitamin K epoxide reductase: homology, active site and catalytic mechanism. Trends Biochem. Sci. 29, 289-292 (2004).
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 289-292
    • Goodstadt, L.1    Ponting, C.P.2
  • 11
    • 47049096139 scopus 로고    scopus 로고
    • Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms
    • Singh, A. K., Bhattacharyya-Pakrasi, M. & Pakrasi, H. B. Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms. J. Biol. Chem. 283, 15762-15770 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 15762-15770
    • Singh, A.K.1    Bhattacharyya-Pakrasi, M.2    Pakrasi, H.B.3
  • 12
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Dutton, R. J., Boyd, D., Berkmen, M. & Beckwith, J. Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc. Natl Acad. Sci. USA 105, 11933-11938 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 13
    • 1342304093 scopus 로고    scopus 로고
    • DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation
    • Inaba, K. et al. DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. J. Biol. Chem. 279, 6761-6768 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 6761-6768
    • Inaba, K.1
  • 14
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba, K. et al. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127, 789-801 (2006).
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1
  • 15
    • 76249133943 scopus 로고    scopus 로고
    • Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin
    • doi:10.1073/pnas.0912952107 15 December
    • Dutton, R. J. et al. Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin. Proc. Natl Acad. Sci. USA advance online publication, doi:10.1073/pnas.0912952107 (15 December 2009).
    • (2009) Proc. Natl Acad. Sci. USA Advance Online Publication
    • Dutton, R.J.1
  • 16
    • 18144423143 scopus 로고    scopus 로고
    • Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation
    • Tie, J. K., Nicchitta, C., von Heijne, G. & Stafford, D. W. Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/ cotranslocation. J. Biol. Chem. 280, 16410-16416 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 16410-16416
    • Tie, J.K.1    Nicchitta, C.2    Von Heijne, G.3    Stafford, D.W.4
  • 17
    • 61449103718 scopus 로고    scopus 로고
    • Novel mutations in the VKORC1 gene of wild rats and mice-a response to 50 years of selection pressure by warfarin?
    • Rost, S. et al. Novel mutations in the VKORC1 gene of wild rats and mice-a response to 50 years of selection pressure by warfarin? BMC Genet. 10, 4 (2009).
    • (2009) BMC Genet. , vol.10 , pp. 4
    • Rost, S.1
  • 18
    • 25444450735 scopus 로고    scopus 로고
    • The genetic basis of resistance to anticoagulants in rodents
    • Pelz, H. J. et al. The genetic basis of resistance to anticoagulants in rodents. Genetics 170, 1839-1847 (2005).
    • (2005) Genetics , vol.170 , pp. 1839-1847
    • Pelz, H.J.1
  • 19
    • 27144553194 scopus 로고    scopus 로고
    • Site-directed mutagenesis of coumarin-type anticoagulant-sensitive VKORC1: Evidence that highly conserved amino acids define structural requirements for enzymatic activity and inhibition by warfarin
    • Rost, S. et al. Site-directed mutagenesis of coumarin-type anticoagulant-sensitive VKORC1: evidence that highly conserved amino acids define structural requirements for enzymatic activity and inhibition by warfarin. Thromb. Haemost. 94, 780-786 (2005).
    • (2005) Thromb. Haemost. , vol.94 , pp. 780-786
    • Rost, S.1
  • 20
    • 33845545299 scopus 로고    scopus 로고
    • A new vitamin K epoxide reductase complex subunit-1 (VKORC1) mutation in a patient with decreased stability of CYP2C9 enzyme
    • D'Ambrosio, R. L., D'Andrea, G., Cafolla, A., Faillace, F. & Margaglione, M. A new vitamin K epoxide reductase complex subunit-1 (VKORC1) mutation in a patient with decreased stability of CYP2C9 enzyme. J. Thromb. Haemost. 5, 191-193 (2007).
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 191-193
    • D'Ambrosio, R.L.1    D'Andrea, G.2    Cafolla, A.3    Faillace, F.4    Margaglione, M.5
  • 21
    • 0019782217 scopus 로고
    • Chemical model studies for the mechanism of vitamin K epoxide reductase
    • Silverman, R. B. Chemical model studies for the mechanism of vitamin K epoxide reductase. J. Am. Chem. Soc. 103, 5939-5941 (1981).
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 5939-5941
    • Silverman, R.B.1
  • 22
    • 2542475140 scopus 로고    scopus 로고
    • Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
    • Gross, E., Kastner, D. B., Kaiser, C. A. & Fass, D. Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117, 601-610 (2004).
    • (2004) Cell , vol.117 , pp. 601-610
    • Gross, E.1    Kastner, D.B.2    Kaiser, C.A.3    Fass, D.4
  • 23
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • Gross, E., Sevier, C. S., Vala, A., Kaiser, C. A. & Fass, D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nature Struct. Biol. 9, 61-67 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 24
    • 33846919393 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of novel warfarin derivatives
    • Gebauer, M. Synthesis and structure-activity relationships of novel warfarin derivatives. Bioorg. Med. Chem. 15, 2414-2420 (2007).
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2414-2420
    • Gebauer, M.1
  • 25
    • 34250796202 scopus 로고    scopus 로고
    • The conversion of vitamin K epoxide to vitamin K quinone and vitamin K quinone to vitamin K hydroquinone uses the same active site cysteines
    • Jin, D. Y., Tie, J. K. & Stafford, D. W. The conversion of vitamin K epoxide to vitamin K quinone and vitamin K quinone to vitamin K hydroquinone uses the same active site cysteines. Biochemistry 46, 7279-7283 (2007).
    • (2007) Biochemistry , vol.46 , pp. 7279-7283
    • Jin, D.Y.1    Tie, J.K.2    Stafford, D.W.3
  • 26
    • 0027475212 scopus 로고
    • A pathway for disulfide bond formation in vivo
    • Bardwell, J. C. et al. A pathway for disulfide bond formation in vivo. Proc. Natl Acad. Sci. USA 90, 1038-1042 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1038-1042
    • Bardwell, J.C.1
  • 27
    • 0032562757 scopus 로고    scopus 로고
    • Reconstitution of a protein disulfide catalytic system
    • Bader, M., Muse, W., Zander, T. & Bardwell, J. Reconstitution of a protein disulfide catalytic system. J. Biol. Chem. 273, 10302-10307 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10302-10307
    • Bader, M.1    Muse, W.2    Zander, T.3    Bardwell, J.4
  • 28
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • Kishigami, S., Kanaya, E., Kikuchi, M. & Ito, K. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J. Biol. Chem. 270, 17072-17074 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17072-17074
    • Kishigami, S.1    Kanaya, E.2    Kikuchi, M.3    Ito, K.4
  • 29
    • 54549124476 scopus 로고    scopus 로고
    • Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
    • Malojcic, G., Owen, R. L., Grimshaw, J. P. & Glockshuber, R. Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB. FEBS Lett. 582, 3301-3307 (2008).
    • (2008) FEBS Lett. , vol.582 , pp. 3301-3307
    • Malojcic, G.1    Owen, R.L.2    Grimshaw, J.P.3    Glockshuber, R.4
  • 30
    • 52049098074 scopus 로고    scopus 로고
    • NMR solution structure of the integral membrane enzyme DsbB: Functional insights into DsbB-catalyzed disulfide bond formation
    • Zhou, Y. et al. NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation. Mol. Cell 31, 896-908 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 896-908
    • Zhou, Y.1
  • 31
    • 62649151322 scopus 로고    scopus 로고
    • Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB
    • Inaba, K. et al. Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB. EMBO J. 28, 779-791 (2009).
    • (2009) EMBO J. , vol.28 , pp. 779-791
    • Inaba, K.1
  • 32
    • 0345133346 scopus 로고    scopus 로고
    • Disulfide bond formation involves a quinhydrone-type charge-transfer complex
    • Regeimbal, J. et al. Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc. Natl Acad. Sci. USA 100, 13779-13784 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13779-13784
    • Regeimbal, J.1
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D 55, 849-861 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 35
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K. D. & Main, P. Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D 52, 43-48 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 36
    • 0030817618 scopus 로고    scopus 로고
    • Combining constraints for electron-density modification
    • Zhang, K. Y., Cowtan, K. & Main, P. Combining constraints for electron-density modification. Methods Enzymol. 277, 53-64 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 53-64
    • Zhang, K.Y.1    Cowtan, K.2    Main, P.3
  • 37
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G. M. A short history of SHELX. Acta Crystallogr. A 64, 112-122 (2008).
    • (2008) Acta Crystallogr. , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 38
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S. & Perrakis, A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nature Protocols 3, 1171-1179 (2008).
    • (2008) Nature Protocols , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 39
    • 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, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N. & Murshudov, G. N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D 57, 122-133 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu, B. P., Ho-Schleyer, S. C., Travers, K. J. & Weissman, J. S. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290, 1571-1574 (2000).
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.