Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution

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...

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Veröffentlicht in:	The Journal of biological chemistry 1990-08, Vol.265 (23), p.14016-14022
Hauptverfasser:	Walter, M R, Cook, W J, Cole, L B, Short, S A, Koszalka, G W, Krenitsky, T A, Ealick, S E
Format:	Artikel
Sprache:	eng
Schlagworte:	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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