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Structure paper

TitleInteractions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase.
Journal, issue, pagesJ. Mol. Biol., Vol. 335, Page 905-921, Year 2004
Publish dateApr 11, 2003 (structure data deposition date)
AuthorsCanyuk, B. / Medrano, F.J. / Wenck, M.A. / Focia, P.J. / Eakin, A.E. / Craig III, S.P.
External linksJ. Mol. Biol. / PubMed:14698288
MethodsX-ray diffraction
Resolution2 - 2.7 Å
Structure data

PDB-1p17:
Hypoxanthine Phosphoribosyltransferase from Trypanosoma cruzi, K68R mutant, complexed with the product IMP
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-1p18:
Hypoxanthine Phosphoribosyltransferase from Trypanosoma cruzi, K68R mutant, ternary substrates complex
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1p19:
Hypoxanthine Phosphoribosyltransferase from Trypanosoma cruzi, in complex with the product IMP
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-IMP:
INOSINIC ACID

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-7HP:
7-HYDROXY-PYRAZOLO[4,3-D]PYRIMIDINE

ChemComp-PRP:
1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose

Source
  • trypanosoma cruzi (eukaryote)
KeywordsTRANSFERASE / GLYCOSYLTRANSFERASE / PHOSPHORIBOSYLTRANSFERASE / NUCLEOTIDE METABOLISM / PURINE SALVAGE / PRODUCT COMPLEX / TERNARY COMPLEX

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