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Structure paper

TitleEvolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas campestris.
Journal, issue, pagesBiochemistry, Vol. 45, Page 14582-14597, Year 2006
Publish dateAug 3, 2006 (structure data deposition date)
AuthorsYew, W.S. / Fedorov, A.A. / Fedorov, E.V. / Rakus, J.F. / Pierce, R.W. / Almo, S.C. / Gerlt, J.A.
External linksBiochemistry / PubMed:17144652
MethodsX-ray diffraction
Resolution1.7 - 1.8 Å
Structure data

PDB-2hxt:
Crystal structure of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and D-erythronohydroxamate
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-2hxu:
Crystal structure of K220A mutant of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and L-fuconate
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-EHM:
(2R,3R)-N,2,3,4-TETRAHYDROXYBUTANAMIDE

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-LFC:
6-deoxy-L-galactonic acid

Source
  • xanthomonas campestris pv. campestris (bacteria)
KeywordsUNKNOWN FUNCTION / L-fuconate dehydratase / enolase superfamily / D-erythromohydroxamate / L-fuconate

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