1tpt

From Proteopedia

THREE-DIMENSIONAL STRUCTURE OF THYMIDINE PHOSPHORYLASE FROM ESCHERICHIA COLI AT 2.8 ANGSTROMS RESOLUTION

Overview

The three-dimensional structure of thymidine phosphorylase from, Escherichia coli has been determined at 2.8 A resolution using, multiple-isomorphous-replacement techniques. The amino acid sequence, deduced from the deoA DNA sequence is also reported. Thymidine, phosphorylase exists in the crystal as an S-shaped dimer in which the, subunits are related by a crystallographic 2-fold axis. Each subunit is, composed of a small alpha-helical domain of six helices and a large, alpha/beta domain. The alpha/beta domain includes a six-stranded mixed, beta-sheet and a four-stranded antiparallel beta-sheet. The active site, has been identified by difference Fourier analyses of the binding of, thymine and thymidine and lies in a cavity between the small and large, domains. The central beta-sheet is splayed open to accommodate a putative, phosphate-binding site which is probably occupied by a sulfate ion in the, crystal.

About this Structure

1TPT is a Single protein structure of sequence from Escherichia coli with SO4 and TDR as ligands. Active as Thymidine phosphorylase, with EC number 2.4.2.4 Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution., Walter MR, Cook WJ, Cole LB, Short SA, Koszalka GW, Krenitsky TA, Ealick SE, J Biol Chem. 1990 Aug 15;265(23):14016-22. PMID:2199449

Page seeded by OCA on Wed Nov 21 03:29:41 2007