1TPT

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

Summary for 1TPT

• Entry DOI: 10.2210/pdb1tpt/pdb
• Descriptor: THYMIDINE PHOSPHORYLASE, SULFATE ION, THYMINE (3 entities in total)
• Functional Keywords: thymidine phosphorylase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 47463.16

Authors

Walter, M.R.,Cook, W.J.,Cole, L.B.,Short, S.A.,Koszalka, G.W.,Krenitsky, T.A.,Ealick, S.E. (deposition date: 1990-06-14, release date: 1991-07-15, Last modification date: 2024-02-14)

Primary citation

Walter, M.R.,Cook, W.J.,Cole, L.B.,Short, S.A.,Koszalka, G.W.,Krenitsky, T.A.,Ealick, S.E.
Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution.
J.Biol.Chem., 265:14016-14022, 1990

PubMed Abstract: 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.

PubMed: 2199449

Experimental method

X-RAY DIFFRACTION (2.8 Å)