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TitleThe structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits.
Journal, issue, pagesBiochemistry, Vol. 38, Page 13829-13836, Year 1999
Publish dateApr 8, 1999 (structure data deposition date)
AuthorsAnderson, A.C. / O'Neil, R.H. / DeLano, W.L. / Stroud, R.M.
External linksBiochemistry / PubMed:10529228
MethodsX-ray diffraction
Resolution2.6 Å
Structure data

PDB-1ci7:
TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

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

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

ChemComp-HOH:
WATER

Source
  • pneumocystis carinii (fungus)
KeywordsTRANSFERASE / METHYLTRANSFERASE / NUCLEOTIDE BIOSYNTHESIS / HALF-SITES REACTIVITY

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