1tpt: Difference between revisions
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|PDB= 1tpt |SIZE=350|CAPTION= <scene name='initialview01'>1tpt</scene>, resolution 2.8Å | |PDB= 1tpt |SIZE=350|CAPTION= <scene name='initialview01'>1tpt</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TDR:THYMINE'>TDR</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Thymidine_phosphorylase Thymidine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.4 2.4.2.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidine_phosphorylase Thymidine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.4 2.4.2.4] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tpt OCA], [http://www.ebi.ac.uk/pdbsum/1tpt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tpt RCSB]</span> | |||
}} | }} | ||
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[[Category: Short, S A.]] | [[Category: Short, S A.]] | ||
[[Category: Walter, M R.]] | [[Category: Walter, M R.]] | ||
[[Category: thymidine phosphorylase]] | [[Category: thymidine phosphorylase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:59:24 2008'' | ||
Revision as of 20:59, 30 March 2008
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| 1tpt, resolution 2.8Å | |||||||||||||
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| Ligands: | SO4, TDR | ||||||||||||
| Activity: | Thymidine phosphorylase, with EC number 2.4.2.4 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
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