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TitleExplaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase.
Journal, issue, pagesBiochemistry, Vol. 47, Page 8902-8911, Year 2008
Publish dateJun 26, 2008 (structure data deposition date)
AuthorsMartucci, W.E. / Vargo, M.A. / Anderson, K.S.
External linksBiochemistry / PubMed:18672899
MethodsX-ray diffraction
Resolution2.74 - 3.25 Å
Structure data

PDB-3dl5:
Crystal Structure of the A287F Active Site Mutant of TS-DHFR from Cryptosporidium hominis
Method: X-RAY DIFFRACTION / Resolution: 2.74 Å

PDB-3dl6:
Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

Chemicals

ChemComp-UMP:
2'-DEOXYURIDINE 5'-MONOPHOSPHATE

ChemComp-CB3:
10-PROPARGYL-5,8-DIDEAZAFOLIC ACID

ChemComp-DHF:
DIHYDROFOLIC ACID

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-HOH:
WATER

Source
  • cryptosporidium hominis (eukaryote)
KeywordsOXIDOREDUCTASE / Enzyme active site mutant / Enzyme-ligand complex

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