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TitleCrystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.
Journal, issue, pagesJ. Biol. Chem., Vol. 281, Page 7533-7545, Year 2006
Publish dateDec 24, 2004 (structure data deposition date)
AuthorsForouhar, F. / Hussain, M. / Farid, R. / Benach, J. / Abashidze, M. / Edstrom, W.C. / Vorobiev, S.M. / Xiao, R. / Acton, T.B. / Fu, Z. ...Forouhar, F. / Hussain, M. / Farid, R. / Benach, J. / Abashidze, M. / Edstrom, W.C. / Vorobiev, S.M. / Xiao, R. / Acton, T.B. / Fu, Z. / Kim, J.J. / Miziorko, H.M. / Montelione, G.T. / Hunt, J.F.
External linksJ. Biol. Chem. / PubMed:16330546
MethodsX-ray diffraction
Resolution2.3 - 2.71 Å
Structure data

PDB-1ydn:
Crystal Structure of the HMG-CoA Lyase from Brucella melitensis, Northeast Structural Genomics Target LR35.
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1ydo:
Crystal Structure of the Bacillis subtilis HMG-CoA Lyase, Northeast Structural Genomics Target SR181.
Method: X-RAY DIFFRACTION / Resolution: 2.71 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-IOD:
IODIDE ION

Source
  • brucella melitensis (bacteria)
  • bacillus subtilis subsp. subtilis (bacteria)
KeywordsLYASE / TIM-barrel protein / Structural Genomics / PSI / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG

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