1tpt | pdb_00001tpt
|
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 Thu Feb 21 15:16:04 2008
