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Structure paper

TitleEvolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2.
Journal, issue, pagesBiochemistry, Vol. 46, Page 9564-9577, Year 2007
Publish dateApr 27, 2007 (structure data deposition date)
AuthorsYew, W.S. / Fedorov, A.A. / Fedorov, E.V. / Almo, S.C. / Gerlt, J.A.
External linksBiochemistry / PubMed:17649980
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-2pp0:
Crystal structure of L-talarate/galactarate dehydratase from Salmonella typhimurium LT2
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2pp1:
Crystal structure of L-talarate/galactarate dehydratase from Salmonella typhimurium LT2 liganded with Mg and L-lyxarohydroxamate
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2pp3:
Crystal structure of L-talarate/galactarate dehydratase mutant K197A liganded with Mg and L-glucarate
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-LLH:
(2R,3S,4R)-2,3,4-TRIHYDROXY-5-(HYDROXYAMINO)-5-OXOPENTANOIC ACID

ChemComp-LGT:
L-GLUCARIC ACID

Source
  • salmonella typhimurium (bacteria)
KeywordsLYASE / Enolase superfamily / L-talarate/Galactarate Dehydratase

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