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TitleCatalytic mechanism and allosteric regulation of UDP-glucose pyrophosphorylase from Leishmania major
Journal, issue, pagesACS CATALYSIS, Vol. 3, Page 2976-2985, Year 2013
Publish dateAug 5, 2013 (structure data deposition date)
AuthorsFuehring, J.I. / Routier, F.H. / Lamerz, A.-C. / Baruch, P. / Gerardy-Schahn, R. / Fedorov, R.
External linksACS CATALYSIS / Search PubMed
MethodsX-ray diffraction
Resolution3 Å
Structure data

PDB-4m28:
UDP-Glucose Pyrophosphorylase from Leishmania major in complex with UTP analog dUpCpp
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-UPC:
2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]uridine

ChemComp-HOH:
WATER

Source
  • leishmania major (eukaryote)
KeywordsTRANSFERASE / UDP-glucose pyrophosphorylase / nucleotidyltransferase / Rossmann-like alpha/beta/alpha sandwich fold

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