1tpt: Difference between revisions

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[[Image:1tpt.jpg|left|200px]]
{{Seed}}
[[Image:1tpt.png|left|200px]]


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{{STRUCTURE_1tpt|  PDB=1tpt  |  SCENE=  }}  
{{STRUCTURE_1tpt|  PDB=1tpt  |  SCENE=  }}  


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




==Overview==
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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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{{ABSTRACT_PUBMED_2199449}}


==About this Structure==
==About this Structure==
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[[Category: Walter, M R.]]
[[Category: Walter, M R.]]
[[Category: Thymidine phosphorylase]]
[[Category: Thymidine phosphorylase]]
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Revision as of 06:06, 29 July 2008

File:1tpt.png

Template:STRUCTURE 1tpt

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

Template:ABSTRACT PUBMED 2199449

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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