Structure of the Y94F mutant of Escherichia coli thymidylate synthase

Sue A. Roberts, David C. Hyatt, Jerry E. Honts, Liming Changchien, Gladys F. Maley, Frank Maley, William R. Montfort

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2′-deoxyuridine 5′-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5′-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.

Original languageEnglish (US)
Pages (from-to)840-843
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number9
StatePublished - Sep 2006

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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