메뉴 건너뛰기




Volumn 194, Issue 3, 2012, Pages 157-166

Crystal structure of the complex between 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum and CoA

Author keywords

Coenzyme A; Crystal structure; Enzyme complex

Indexed keywords

4 HYDROXYBUTYRATE COENZYME A TRANSFERASE; ACID ANHYDRIDE; COENZYME A; COENZYME A TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84857915081     PISSN: 03028933     EISSN: 1432072X     Source Type: Journal    
DOI: 10.1007/s00203-011-0737-2     Document Type: Article
Times cited : (4)

References (30)
  • 1
    • 0028103275 scopus 로고
    • The Ccp4 suite - Programs for protein crystallography
    • Bailey S (1994) The Ccp4 suite - programs for protein crystallography. Acta Crystallogr Sect. D-Biol Crystallogr 50:760-763
    • (1994) Acta Crystallogr Sect. D-Biol Crystallogr , vol.50 , pp. 760-763
    • Bailey, S.1
  • 2
    • 2242445271 scopus 로고    scopus 로고
    • Structure of the mammalian CoA transferase from pig heart
    • DOI 10.1021/bi020568f
    • Bateman KS, Brownie ER, Wolodko WT, Fraser ME (2002) Structure of the mammalian CoA transferase from pig heart. Biochemistry 41:14455-14462 (Pubitemid 35440256)
    • (2002) Biochemistry , vol.41 , Issue.49 , pp. 14455-14462
    • Bateman, K.S.1    Brownie, E.R.2    Wolodko, W.T.3    Fraser, M.E.4
  • 3
    • 44449097276 scopus 로고    scopus 로고
    • Reinvestigation of the catalytic mechanism of formyl-CoA transferase, a class III CoA-transferase
    • Berthold CL, Toyota CG, Richards NGJ, Lindqvist Y (2008) Reinvestigation of the catalytic mechanism of formyl-CoA transferase, a class III CoA-transferase. J Biol Chem 283:65196529
    • (2008) J Biol Chem , vol.283 , pp. 65196529
    • Berthold, C.L.1    Toyota, C.G.2    Richards, N.G.J.3    Lindqvist, Y.4
  • 4
    • 0014689979 scopus 로고
    • Role of a buried acid group in mechanism of action of chymotrypsin
    • Blow DM, Birktoft JJ, Hartley BS (1969) Role of a buried acid group in mechanism of action of chymotrypsin. Nature 221:337-340
    • (1969) Nature , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartley, B.S.3
  • 5
    • 0019401061 scopus 로고
    • Glutaconate coenzyme A transferase from Acidaminococcus-fermentans
    • Buckel W, Dorn U, Semmler R (1981) Glutaconate coenzyme A transferase from Acidaminococcus-fermentans. Eur J Biochem 118:315-322
    • (1981) Eur J Biochem , vol.118 , pp. 315-322
    • Buckel, W.1    Dorn, U.2    Semmler, R.3
  • 7
    • 0033849869 scopus 로고    scopus 로고
    • Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: Cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA
    • Gerhardt A, Cinkaya I, Linder D, Huisman G, Buckel W (2000) Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA. Arch Microbiol 174:189-199
    • (2000) Arch Microbiol , vol.174 , pp. 189-199
    • Gerhardt, A.1    Cinkaya, I.2    Linder, D.3    Huisman, G.4    Buckel, W.5
  • 8
    • 0035861886 scopus 로고    scopus 로고
    • A new family of CoA-transferases
    • Heider J (2001) A new family of CoA-transferases. FEBS Lett 509:345-349
    • (2001) FEBS Lett , vol.509 , pp. 345-349
    • Heider, J.1
  • 9
    • 0031569327 scopus 로고    scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans: The crystal structure reveals homology with other CoA-transferases
    • Jacob U, Mack M, Clausen T, Huber R, Buckel W, Messerschmidt A (1997) Glutaconate CoA-transferase from Acidaminococcus fermentans - the crystal structure reveals homology with other CoA-transferases. Structure 5:415-426 (Pubitemid 27169942)
    • (1997) Structure , vol.5 , Issue.3 , pp. 415-426
    • Jacob, U.1    Mack, M.2    Clausen, T.3    Huber, R.4    Buckel, W.5    Messerschmidt, A.6
  • 10
    • 77956933889 scopus 로고
    • Coenzyme A transferases
    • Boyer PD (ed) Academic Press, New York
    • Jencks WP (1973) Coenzyme A transferases. In: Boyer PD (ed) The enzymes. Academic Press, New York, pp 483-496
    • (1973) The Enzymes , pp. 483-496
    • Jencks, W.P.1
  • 11
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W (1976) A solution for the best rotation to relate two sets of vectors. Acta Crystallogr Sect. A 32:922-923
    • (1976) Acta Crystallogr Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 13
    • 33748771961 scopus 로고    scopus 로고
    • Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by clostridium difficile
    • DOI 10.1128/AEM.00772-06
    • Kim J, Darley D, Selmer T, Buckel W (2006) Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl Environ Microbiol 72:6062-6069 (Pubitemid 44414637)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.9 , pp. 6062-6069
    • Kim, J.1    Darley, D.2    Selmer, T.3    Buckel, W.4
  • 14
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr Sect. D 60:2256-2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 I , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 15
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • DOI 10.1006/jmbi.1993.1351
    • Laskowski RA, Moss DS, Thornton JM (1993) Main-chain bond lengths and bond angles in protein structures. J Mol Biol 231:1049-1067 (Pubitemid 23209879)
    • (1993) Journal of Molecular Biology , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 16
    • 77952837412 scopus 로고    scopus 로고
    • Sampling long time scale protein motions: OSRW simulation of active site loop conformational free energies in formyl-CoA:Oxalate CoA transferase
    • Lee S, Chen M, Yang W, Richards NG (2010) Sampling long time scale protein motions: OSRW simulation of active site loop conformational free energies in formyl-CoA:oxalate CoA transferase. J Am Chem Soc 132:7252-7253
    • (2010) J Am Chem Soc , vol.132 , pp. 7252-7253
    • Lee, S.1    Chen, M.2    Yang, W.3    Richards, N.G.4
  • 17
    • 72949097050 scopus 로고    scopus 로고
    • Crystal Structure of 4-Hydroxybutyrate CoA-Transferase from Clostridium aminobutyricum
    • Macieira S, Zhang J, Velarde M, Buckel W, Messerschmidt A (2009) Crystal Structure of 4-Hydroxybutyrate CoA-Transferase from Clostridium aminobutyricum. Biol Chem 390:1251-1263
    • (2009) Biol Chem , vol.390 , pp. 1251-1263
    • Macieira, S.1    Zhang, J.2    Velarde, M.3    Buckel, W.4    Messerschmidt, A.5
  • 18
    • 24644488646 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif
    • Messerschmidt Aet al (2005) Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. J Mol Biol 352:918-931
    • (2005) J Mol Biol , vol.352 , pp. 918-931
    • Messerschmidt, A.1
  • 19
    • 0002580781 scopus 로고    scopus 로고
    • Simplified error estimation a la Cruickshank in macromolecular crystallography
    • Murshudov GN, Dodson EJ (1997) Simplified error estimation a la Cruickshank in macromolecular crystallography. CCP4 Newslett Protein Crystallogr 33:31-39
    • (1997) CCP4 Newslett Protein Crystallogr , vol.33 , pp. 31-39
    • Murshudov, G.N.1    Dodson, E.J.2
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 79955374524 scopus 로고    scopus 로고
    • Substrate specificity of 2-hydroxyglutaryl-CoA dehydratase from clostridium symbiosum: Toward a bio-based production of adipic acid
    • Parthasarathy A, Pierik AJ, Kahnt J, Zelder O, Buckel W (2011a) Substrate specificity of 2-hydroxyglutaryl-CoA dehydratase from clostridium symbiosum: toward a bio-based production of adipic acid. Biochemistry 50:3540-3550
    • (2011) Biochemistry , vol.50 , pp. 3540-3550
    • Parthasarathy, A.1    Pierik, A.J.2    Kahnt, J.3    Zelder, O.4    Buckel, W.5
  • 23
    • 79956210880 scopus 로고    scopus 로고
    • Correction to substrate specificity of 2-hydroxyglutaryl-CoA dehydratase from clostridium symbiosum: Toward a Bio-based production of adipic acid
    • Parthasarathy A, Pierik AJ, Kahnt J, Zelder O, Buckel W (2011b) Correction to substrate specificity of 2-hydroxyglutaryl-CoA dehydratase from clostridium symbiosum: toward a Bio-based production of adipic acid. Biochemistry 50:4392
    • (2011) Biochemistry , vol.50 , pp. 4392
    • Parthasarathy, A.1    Pierik, A.J.2    Kahnt, J.3    Zelder, O.4    Buckel, W.5
  • 26
    • 0025780688 scopus 로고
    • Purification and properties of 4 hydroxybutyrate coenzyme A transferase from Clostridium aminobutyricum
    • Scherf U, Buckel W (1991) Purification and properties of 4 hydroxybutyrate coenzyme A transferase from Clostridium aminobutyricum. Appl Environ Microbiol 57:2699-2702
    • (1991) Appl Environ Microbiol , vol.57 , pp. 2699-2702
    • Scherf, U.1    Buckel, W.2
  • 27
    • 0036151093 scopus 로고    scopus 로고
    • Propionate CoA-transferase from Clostridium propionicum: Cloning of the gene and identification of glutamate 324 at the active site
    • DOI 10.1046/j.0014-2956.2001.02659.x
    • Selmer T, Willanzheimer A, Hetzel M (2002) Propionate CoA-transferase from Clostridium propionicum. Cloning of gene and identification of glutamate 324 at the active site. Eur J Biochem 269:372-380 (Pubitemid 34107372)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.1 , pp. 372-380
    • Selmer, T.1    Willanzheimer, A.2    Hetzel, M.3
  • 28
    • 0000060558 scopus 로고
    • The preparation of S-succinyl coenzyme A
    • Simon EJ, Shemin D (1953) The preparation of S-succinyl coenzyme A. J Am Chem Soc 75:2520
    • (1953) J Am Chem Soc , vol.75 , pp. 2520
    • Simon, E.J.1    Shemin, D.2
  • 29
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A (1997) Molrep - an automated program for molecular replacement. J Appl Crystallogr 30:1022-1025 (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 0017290637 scopus 로고
    • Mechanism and specificity of succinyl-CoA:3-ketoacid coenzyme A transferase
    • White H, Jencks WP (1976) Mechanism and specificity of succinyl-CoA:3-ketoacid coenzyme A transferase. J Biol Chem 251:1688-1699
    • (1976) J Biol Chem , vol.251 , pp. 1688-1699
    • White, H.1    Jencks, W.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.