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1tpt
From Proteopedia
(New page: 200px<br /><applet load="1tpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tpt, resolution 2.8Å" /> '''THREE-DIMENSIONAL STR...) |
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| - | [[Image:1tpt.jpg|left|200px]]<br /><applet load="1tpt" size=" | + | [[Image:1tpt.jpg|left|200px]]<br /><applet load="1tpt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tpt, resolution 2.8Å" /> | caption="1tpt, resolution 2.8Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF THYMIDINE PHOSPHORYLASE FROM ESCHERICHIA COLI AT 2.8 ANGSTROMS RESOLUTION'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF THYMIDINE PHOSPHORYLASE FROM ESCHERICHIA COLI AT 2.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of thymidine phosphorylase from | + | 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== | ==About this Structure== | ||
| - | 1TPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and TDR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1TPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=TDR:'>TDR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thymidine phosphorylase]] | [[Category: Thymidine phosphorylase]] | ||
| - | [[Category: Cole, L | + | [[Category: Cole, L B.]] |
| - | [[Category: Cook, W | + | [[Category: Cook, W J.]] |
| - | [[Category: Ealick, S | + | [[Category: Ealick, S E.]] |
| - | [[Category: Koszalka, G | + | [[Category: Koszalka, G W.]] |
| - | [[Category: Krenitsky, T | + | [[Category: Krenitsky, T A.]] |
| - | [[Category: Short, S | + | [[Category: Short, S A.]] |
| - | [[Category: Walter, M | + | [[Category: Walter, M R.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: TDR]] | [[Category: TDR]] | ||
[[Category: thymidine phosphorylase]] | [[Category: thymidine phosphorylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:04 2008'' |
Revision as of 13:16, 21 February 2008
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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 with and as ligands. Active as Thymidine phosphorylase, with EC number 2.4.2.4 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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