2tdm

From Proteopedia

Revision as of 16:01, 29 October 2007

STRUCTURE OF THYMIDYLATE SYNTHASE

Overview

Crystal structures of two crystal forms of the complex of Lactobacillus, casei (TS) with its substrate dUMP have been solved and refined at 2.55 A, resolution. The two crystal forms differ by approximately 5% in the c-axis, length. The TS-dUMP complexes are symmetric dimers with dUMP bound, equivalently in both active sites. dUMP is non-covalently bound in the, same conformation as in ternary complexes of TS with dUMP and cofactor or, cofactor analogs. The same hydrogen bonds are made between TS and, substrate in the binary and ternary complexes. We have also determined the, 2.36 A crystal structure of phosphate-bound L. casei TS. This structure, has been refined to an R-factor of 19.3% with highly constrained geometry., Refinement has revealed the locations of all residues in the ... [(full description)]

About this Structure

2TDM is a [Single protein] structure of sequence from [Lactobacillus casei] with UMP as [ligand]. This structure superseeds the now removed PDB entry 1TDM. Active as [[1]], with EC number [2.1.1.45]. Full crystallographic information is available from [OCA].

Reference

Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei., Finer-Moore J, Fauman EB, Foster PG, Perry KM, Santi DV, Stroud RM, J Mol Biol. 1993 Aug 20;232(4):1101-16. PMID:8371269

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