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TitleCatalytic Mechanism and Allosteric Regulation of Udp-Glucose Pyrophosphorylase from Leishmania Major
Journal, issue, pagesACS CATALYSIS, Vol. 3, Page 2161-2985, Year 2013
Publish dateAug 5, 2013 (structure data deposition date)
AuthorsFuehring, J. / Routier, F.H. / Lamerz, A.-C. / Baruch, P. / Gerardy-Schahn, R. / Fedorov, R.
External linksACS CATALYSIS / Search PubMed
MethodsX-ray diffraction
Resolution1.66 - 2.2 Å
Structure data

PDB-4m2a:
Crystal structure of the udp-glucose pyrophosphorylase from Leishmania major in the post-reactive state
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

PDB-4m2b:
Crystal structure of L281D mutant of udp-glucose pyrophosphorylase from leishmania major in complex with udp-glc
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-UPG:
URIDINE-5'-DIPHOSPHATE-GLUCOSE

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • leishmania major (eukaryote)
KeywordsTRANSFERASE / ROSSMANN-LIKE ALPHA/BETA/ALPHA SANDWICH FOLD / NUCLEOTIDYLTRANSFERASE

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