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Structure paper

TitleDeciphering the enzymatic mechanism of sugar ring contraction in UDP-apiose biosynthesis.
Journal, issue, pagesNat Catal, Vol. 2, Page 1115-1123, Year 2019
Publish dateJul 10, 2018 (structure data deposition date)
AuthorsSavino, S. / Borg, A.J.E. / Dennig, A. / Pfeiffer, M. / de Giorgi, F. / Weber, H. / Dubey, K.D. / Rovira, C. / Mattevi, A. / Nidetzky, B.
External linksNat Catal / PubMed:31844840
MethodsX-ray diffraction
Resolution3.02 - 3.47 Å
Structure data

PDB-6h0n:
The structure of wild-type Arabidopsis thaliana UDP-apiose/UDP-xylose synthase in complex with NAD+ and UDP
Method: X-RAY DIFFRACTION / Resolution: 3.02 Å

PDB-6h0p:
The structure of C100A mutant of Arabidopsis thaliana UDP-apiose/UDP-xylose synthase in complex with NADH and UDP-D-glucuronic acid
Method: X-RAY DIFFRACTION / Resolution: 3.47 Å

Chemicals

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

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-UGA:
URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID

Source
  • arabidopsis thaliana (thale cress)
KeywordsOXIDOREDUCTASE / Enzyme catalysis / glycobiology / short-chain dehydrogenases/reductases (SDR) / aldol cleavage / substrate-assisted reaction

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