PMID:2199449
| Citation |
Walter, MR, Cook, WJ, Cole, LB, Short, SA, Koszalka, GW, Krenitsky, TA and Ealick, SE (1990) Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. J. Biol. Chem. 265:14016-22 |
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| 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. |
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| Keywords |
Amino Acid Sequence; Binding Sites; Cloning, Molecular; Crystallization; DNA, Bacterial/genetics; Escherichia coli/enzymology; Ligands; Models, Molecular; Molecular Sequence Data; Pentosyltransferases/genetics; Pentosyltransferases/isolation & purification; Protein Conformation; Thymidine Phosphorylase/genetics; Thymidine Phosphorylase/isolation & purification; X-Ray Diffraction |
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