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TitleStructural and functional evolution of isopropylmalate dehydrogenases in the leucine and glucosinolate pathways of Arabidopsis thaliana.
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 28794-28801, Year 2011
Publish dateMar 24, 2011 (structure data deposition date)
AuthorsHe, Y. / Galant, A. / Pang, Q. / Strul, J.M. / Balogun, S.F. / Jez, J.M. / Chen, S.
External linksJ. Biol. Chem. / PubMed:21697089
MethodsX-ray diffraction
Resolution2.25 Å
Structure data

PDB-3r8w:
Structure of 3-isopropylmalate dehydrogenase isoform 2 from Arabidopsis thaliana at 2.2 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
KeywordsOXIDOREDUCTASE / dimer / isocitrate and isopropylmalate dehydrogenases family / leucine biosynthesis / glucosinolate biosynthesis / NADH / 3-isopropylmalate / chloroplast

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