Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. 1990

M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
Department of Biochemistry, University of Alabama, Birmingham 35294.

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.

UI MeSH Term Description Entries
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010430 Pentosyltransferases Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another.
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D004269 DNA, Bacterial Deoxyribonucleic acid that makes up the genetic material of bacteria. Bacterial DNA
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
September 1988, Journal of biochemistry,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
June 1975, Proceedings of the National Academy of Sciences of the United States of America,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
June 1985, Proceedings of the National Academy of Sciences of the United States of America,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
November 1985, Journal of molecular biology,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
August 1997, Nature structural biology,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
March 1992, Journal of biochemistry,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
January 1978, Methods in enzymology,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
November 1997, Journal of molecular biology,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
April 1997, Journal of molecular biology,
M R Walter, and W J Cook, and L B Cole, and S A Short, and G W Koszalka, and T A Krenitsky, and S E Ealick
January 1991, Proteins,
Copied contents to your clipboard!