2ftn

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2ftn, resolution 1.60Å

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E. coli thymidylate synthase Y94F mutant

Overview

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.

About this Structure

2FTN is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Active as Thymidylate synthase, with EC number 2.1.1.45 Full crystallographic information is available from OCA.

Reference

Structure of the Y94F mutant of Escherichia coli thymidylate synthase., Roberts SA, Hyatt DC, Honts JE, Changchien L, Maley GF, Maley F, Montfort WR, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):840-3. Epub 2006 Aug 18. PMID:16946460

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