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TitleEnzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination.
Journal, issue, pagesBiol. Chem., Vol. 394, Page 1505-1516, Year 2013
Publish dateSep 22, 2009 (structure data deposition date)
AuthorsHoppner, A. / Schomburg, D. / Niefind, K.
External linksBiol. Chem. / PubMed:23929881
MethodsX-ray diffraction
Resolution1 - 1.16 Å
Structure data

PDB-3jyo:
Quinate dehydrogenase from Corynebacterium glutamicum in complex with NAD
Method: X-RAY DIFFRACTION / Resolution: 1 Å

PDB-3jyp:
Quinate dehydrogenase from Corynebacterium glutamicum in complex with quinate and NADH
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

PDB-3jyq:
Quinate dehydrogenase from Corynebacterium glutamicum in complex with shikimate and NADH
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-QIC:
(1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid

ChemComp-SKM:
(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID

Source
  • corynebacterium glutamicum (bacteria)
KeywordsOXIDOREDUCTASE / enzyme-cofactor complex / Amino-acid biosynthesis / Aromatic amino acid biosynthesis / NAD / quinate dehyrogenase / ternary complex / quinate / NADH / shikimate

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