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Structure paper

TitleIs dimerization required for the catalytic activity of bacterial biotin carboxylase?
Journal, issue, pagesMol. Cell, Vol. 22, Page 807-818, Year 2006
Publish dateApr 18, 2006 (structure data deposition date)
AuthorsShen, Y. / Chou, C.Y. / Chang, G.G. / Tong, L.
External linksMol. Cell / PubMed:16793549
MethodsX-ray diffraction
Resolution2.2 - 2.8 Å
Structure data

PDB-2gps:
Crystal Structure of the Biotin Carboxylase Subunit, E23R mutant, of Acetyl-CoA Carboxylase from Escherichia coli.
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-2gpw:
Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsLIGASE / ATP-grasp / carboxylase / biotin-dependent / fatty acid synthesis / dimer-interface mutant

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