메뉴 건너뛰기




Volumn 13, Issue 12, 2005, Pages 1745-1754

Release of a damaged cofactor from a coenzyme B12-dependent enzyme: X-ray structures of diol dehydratase-reactivating factor

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; COBAMAMIDE; HYDROLYASE; NUCLEOTIDE;

EID: 28844451831     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.08.011     Document Type: Article
Times cited : (27)

References (42)
  • 2
    • 0017575198 scopus 로고
    • Mechanism of action of adenosylcobalamin: Glycerol and other substrate analogues as substrates and inactivators for propanediol dehydratase - Kinetics, stereospecificity, and mechanism
    • W.W. Bachovchin, R.G. Eagar Jr., K.W. Moore, and J.H. Richards Mechanism of action of adenosylcobalamin: glycerol and other substrate analogues as substrates and inactivators for propanediol dehydratase - kinetics, stereospecificity, and mechanism Biochemistry 16 1977 1082 1092
    • (1977) Biochemistry , vol.16 , pp. 1082-1092
    • Bachovchin, W.W.1    Eagar Jr., R.G.2    Moore, K.W.3    Richards, J.H.4
  • 3
    • 0004247468 scopus 로고    scopus 로고
    • John Wiley & Sons New York
    • 12 1999 John Wiley & Sons New York
    • (1999) 12
    • Banerjee, R.1
  • 4
    • 0037899473 scopus 로고    scopus 로고
    • Radical carbon skeleton rearrangements: Catalysis by coenzyme B12-dependent mutases
    • R. Banerjee Radical carbon skeleton rearrangements: catalysis by coenzyme B12-dependent mutases Chem. Rev. 103 2003 2083 2094
    • (2003) Chem. Rev. , vol.103 , pp. 2083-2094
    • Banerjee, R.1
  • 5
    • 0027412196 scopus 로고
    • ALSCRIPT - A tool to format multiple sequence alignments
    • G.J. Barton 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
  • 6
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • P. Bork, C. Sander, and A. Valencia An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins Proc. Natl. Acad. Sci. USA 9 1992 7290 7294
    • (1992) Proc. Natl. Acad. Sci. USA , vol.9 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 8
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • E. de La Fortelle, and G. Bricogne Maximum-likelihood heavy-atom parameter refinement for the 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
  • 10
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein
    • K.M. Flaherty, C. DeLuca-Flaherty, and D.B. McKay Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein Nature 346 1990 623 628
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 11
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • M.M. Harding Geometry of metal-ligand interactions in proteins Acta Crystallogr. D57 2001 401 411
    • (2001) Acta Crystallogr. , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 12
    • 0019213963 scopus 로고
    • In situ reactivation of glycerol-inactivated coenzyme B12-dependent enzymes, glycerol dehydratase and diol dehydratase
    • S. Honda, T. Toraya, and S. Fukui In situ reactivation of glycerol-inactivated coenzyme B12-dependent enzymes, glycerol dehydratase and diol dehydratase J. Bacteriol. 143 1980 1458 1465
    • (1980) J. Bacteriol. , vol.143 , pp. 1458-1465
    • Honda, S.1    Toraya, T.2    Fukui, S.3
  • 13
    • 0035965190 scopus 로고    scopus 로고
    • Characterization and mechanism of action of a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase
    • H. Kajiura, K. Mori, T. Tobimatsu, and T. Toraya Characterization and mechanism of action of a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase J. Biol. Chem. 276 2001 36514 36519
    • (2001) J. Biol. Chem. , vol.276 , pp. 36514-36519
    • Kajiura, H.1    Mori, K.2    Tobimatsu, T.3    Toraya, T.4
  • 14
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, J.1
  • 15
    • 73649177916 scopus 로고
    • Purification and properties of dioldehydrase, an enzyme requiring a cobamide coenzyme
    • H.A. Lee Jr., and R.H. Abeles Purification and properties of dioldehydrase, an enzyme requiring a cobamide coenzyme J. Biol. Chem. 238 1963 2367 2373
    • (1963) J. Biol. Chem. , vol.238 , pp. 2367-2373
    • Lee Jr., H.A.1    Abeles, R.H.2
  • 17
    • 0037225353 scopus 로고    scopus 로고
    • Structure of glycerol dehydratase reactivase: A new type of molecular chaperone
    • D.-I. Liao, L. Reiss, I. Turner Jr., and G. Dotson Structure of glycerol dehydratase reactivase: a new type of molecular chaperone Structure 11 2003 109 119
    • (2003) Structure , vol.11 , pp. 109-119
    • Liao, D.-I.1    Reiss, L.2    Turner Jr., I.3    Dotson, G.4
  • 18
    • 4243468938 scopus 로고    scopus 로고
    • The cation-π interaction
    • J.C. Ma, and D.A. Dougherty The cation-π interaction Chem. Rev. 97 1997 1303 1324
    • (1997) Chem. Rev. , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 19
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 21
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 22
    • 0032855711 scopus 로고    scopus 로고
    • Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor
    • K. Mori, and T. Toraya Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor Biochemistry 38 1999 13170 13178
    • (1999) Biochemistry , vol.38 , pp. 13170-13178
    • Mori, K.1    Toraya, T.2
  • 23
    • 0031240468 scopus 로고    scopus 로고
    • A protein factor is essential for in situ reactivation of glycerol-inactivated adenosylcobalamin-dependent diol dehydratase
    • K. Mori, T. Tobimatsu, and T. Toraya A protein factor is essential for in situ reactivation of glycerol-inactivated adenosylcobalamin-dependent diol dehydratase Biosci. Biotechnol. Biochem. 61 1997 1729 1733
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1729-1733
    • Mori, K.1    Tobimatsu, T.2    Toraya, T.3
  • 24
    • 0031464312 scopus 로고    scopus 로고
    • Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase
    • K. Mori, T. Tobimatsu, T. Hara, and T. Toraya Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase J. Biol. Chem. 272 1997 32034 32041
    • (1997) J. Biol. Chem. , vol.272 , pp. 32034-32041
    • Mori, K.1    Tobimatsu, T.2    Hara, T.3    Toraya, T.4
  • 25
    • 4944253783 scopus 로고    scopus 로고
    • Identification of a reactivating factor for adenosylcobalamin-dependent ethanolamine ammonia lyase
    • K. Mori, R. Bando, N. Hieda, and T. Toraya Identification of a reactivating factor for adenosylcobalamin-dependent ethanolamine ammonia lyase J. Bacteriol. 186 2004 6845 6854
    • (2004) J. Bacteriol. , vol.186 , pp. 6845-6854
    • Mori, K.1    Bando, R.2    Hieda, N.3    Toraya, T.4
  • 26
    • 28844468575 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of molecular chaperone-like diol dehydratase-reactivating factor in ADP-bound and nucleotide-free forms
    • K. Mori, N. Hieda, Y. Yamanishi, N. Shibata, and T. Toraya Crystallization and preliminary X-ray analysis of molecular chaperone-like diol dehydratase-reactivating factor in ADP-bound and nucleotide-free forms Acta Crystallogr. F 61 2005 603 605
    • (2005) Acta Crystallogr. F , vol.61 , pp. 603-605
    • Mori, K.1    Hieda, N.2    Yamanishi, Y.3    Shibata, N.4    Toraya, T.5
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin 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.2    Lamzin, V.S.3
  • 29
    • 0035012408 scopus 로고    scopus 로고
    • Identification and expression of the genes and purification and characterization of the gene products involved in reactivation of coenzyme B12-dependent glycerol dehydratase of Citrobacter freundii
    • C. Seifert, S. Bowien, G. Gottschalk, and R. Daniel Identification and expression of the genes and purification and characterization of the gene products involved in reactivation of coenzyme B12-dependent glycerol dehydratase of Citrobacter freundii Eur. J. Biochem. 268 2001 2369 2378
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2369-2378
    • Seifert, C.1    Bowien, S.2    Gottschalk, G.3    Daniel, R.4
  • 31
    • 0033024922 scopus 로고    scopus 로고
    • Identification and expression of the genes encoding a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase
    • T. Tobimatsu, H. Kajiura, M. Yunoki, M. Azuma, and T. Toraya Identification and expression of the genes encoding a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase J. Bacteriol. 181 1999 4110 4113
    • (1999) J. Bacteriol. , vol.181 , pp. 4110-4113
    • Tobimatsu, T.1    Kajiura, H.2    Yunoki, M.3    Azuma, M.4    Toraya, T.5
  • 32
    • 0001965823 scopus 로고    scopus 로고
    • Diol dehydratase and glycerol dehydratase
    • R. Banerjee John Wiley & Sons New York
    • 12 1999 John Wiley & Sons New York 783 809
    • (1999) 12 , pp. 783-809
    • Toraya, T.1
  • 33
    • 0033624272 scopus 로고    scopus 로고
    • 12-enzymes: Structure, mechanism, inactivation, and reactivation of diol and glycerol dehydratases
    • 12-enzymes: structure, mechanism, inactivation, and reactivation of diol and glycerol dehydratases Cell. Mol. Life Sci. 57 2000 106 127
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 106-127
    • Toraya, T.1
  • 34
    • 0037560995 scopus 로고    scopus 로고
    • 12-dependent isomerization (eliminating) reactions
    • 12-dependent isomerization (eliminating) reactions Chem. Rev. 103 2003 2095 2127
    • (2003) Chem. Rev. , vol.103 , pp. 2095-2127
    • Toraya, T.1
  • 35
    • 0033525074 scopus 로고    scopus 로고
    • 12-dependent diol dehydratase
    • 12-dependent diol dehydratase J. Biol. Chem. 274 1999 3372 3377
    • (1999) J. Biol. Chem. , vol.274 , pp. 3372-3377
    • Toraya, T.1    Mori, K.2
  • 37
    • 0018198342 scopus 로고
    • 12-dependent diol dehydratase: Regulation of apoenzyme synthesis in Klebsiella pneumoniae (Aerobacter aerogenes) ATCC 8724
    • 12- dependent diol dehydratase: regulation of apoenzyme synthesis in Klebsiella pneumoniae (Aerobacter aerogenes) ATCC 8724 J. Bacteriol. 135 1978 726 729
    • (1978) J. Bacteriol. , vol.135 , pp. 726-729
    • Toraya, T.1    Honda, S.2    Kuno, S.3    Fukui, S.4
  • 38
    • 0018908909 scopus 로고
    • 12-dependent diol dehydratase and glycerol dehydratase in selected genera of Enterobacteriaceae and Propionibacteriaceae
    • 12-dependent diol dehydratase and glycerol dehydratase in selected genera of Enterobacteriaceae and Propionibacteriaceae J. Bacteriol. 141 1980 1439 1442
    • (1980) J. Bacteriol. , vol.141 , pp. 1439-1442
    • Toraya, T.1    Kuno, S.2    Fukui, S.3
  • 40
    • 0014027350 scopus 로고
    • Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex
    • O.W. Wagner, H.A. Lee Jr., P.A. Frey, and R.H. Abeles Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex J. Biol. Chem. 241 1966 1751 1762
    • (1966) J. Biol. Chem. , vol.241 , pp. 1751-1762
    • Wagner, O.W.1    Lee Jr., H.A.2    Frey, P.A.3    Abeles, R.H.4
  • 41
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • C.M. Weeks, and R. Miller The design and implementation of SnB v2.0 J. Appl. Crystallogr. 32 1999 120 124
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.