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TitleGlutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.
Journal, issue, pagesFebs Lett., Vol. 589, Page 240-245, Year 2015
Publish dateNov 3, 2014 (structure data deposition date)
AuthorsGraczer, E. / Pallo, A. / Olah, J. / Szimler, T. / Konarev, P.V. / Svergun, D.I. / Merli, A. / Zavodszky, P. / Weiss, M.S. / Vas, M.
External linksFebs Lett. / PubMed:25497013
MethodsX-ray diffraction
Resolution2.05 Å
Structure data

PDB-4wuo:
Structure of the E270A Mutant Isopropylmalate dehydrogenase from Thermus thermophilus in complex with IPM, Mn and NADH
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-IPM:
3-ISOPROPYLMALIC ACID

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-MN:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-EOH:
ETHANOL

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • thermus thermophilus (bacteria)
KeywordsOXIDOREDUCTASE / ISOPROPYLMALATE DEHYDROGENASE / IPMDH / MUTANT

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