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4lhm

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Revision as of 09:47, 4 August 2016

Thymidine phosphorylase from E.coli with 3'-azido-3'-deoxythymidine

Structural highlights

4lhm is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	deoA, tpp, ttg, b4382, JW4345 (ECOLI)
Activity:	Thymidine phosphorylase, with EC number 2.4.2.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TYPH_ECOLI] The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.

Publication Abstract from PubMed

The structural study of complexes of thymidine phosphorylase (TP) with nucleoside analogues which inhibit its activity is of special interest because many of these compounds are used as chemotherapeutic agents. Determination of kinetic parameters showed that 3'-azido-3'-deoxythymidine (3'-azidothymidine; AZT), which is widely used for the treatment of human immunodeficiency virus, is a reversible noncompetitive inhibitor of Escherichia coli thymidine phosphorylase (TP). The three-dimensional structure of E. coli TP complexed with AZT was solved by the molecular-replacement method and was refined at 1.52 A resolution. Crystals for X-ray study were grown in microgravity by the counter-diffusion technique from a solution of the protein in phosphate buffer with ammonium sulfate as a precipitant. The AZT molecule was located with full occupancy in the electron-density maps in the nucleoside-binding pocket of TP, whereas the phosphate-binding pocket of the enzyme was occupied by phosphate (or sulfate) ion. The structure of the active-site cavity and conformational changes of the enzyme upon AZT binding are described in detail. It is found that the position of AZT differs remarkably from the positions of the pyrimidine bases and nucleoside analogues in other known complexes of pyrimidine phosphorylases, but coincides well with the position of 2'-fluoro-3'-azido-2',3'-dideoxyuridine (N3FddU) in the recently investigated complex of E. coli TP with this ligand (Timofeev et al., 2013). The peculiarities of the arrangement of N3FddU and 3'-azidothymidine in the nucleoside binding pocket of TP and correlations between the arrangement and inhibitory properties of these compounds are discussed.

3'-Azidothymidine in the active site of Escherichia coli thymidine phosphorylase: the peculiarity of the binding on the basis of X-ray study.,Timofeev V, Abramchik Y, Zhukhlistova N, Muravieva T, Fateev I, Esipov R, Kuranova I Acta Crystallogr D Biol Crystallogr. 2014 Apr;70(Pt 4):1155-65. doi:, 10.1107/S1399004714001904. Epub 2014 Mar 21. PMID:24699659^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Timofeev V, Abramchik Y, Zhukhlistova N, Muravieva T, Fateev I, Esipov R, Kuranova I. 3'-Azidothymidine in the active site of Escherichia coli thymidine phosphorylase: the peculiarity of the binding on the basis of X-ray study. Acta Crystallogr D Biol Crystallogr. 2014 Apr;70(Pt 4):1155-65. doi:, 10.1107/S1399004714001904. Epub 2014 Mar 21. PMID:24699659 doi:http://dx.doi.org/10.1107/S1399004714001904

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lhm"

@@ Line 1: / Line 1: @@
 ==Thymidine phosphorylase from E.coli with 3'-azido-3'-deoxythymidine==
 <StructureSection load='4lhm' size='340' side='right' caption='[[4lhm]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">deoA, tpp, ttg, b4382, JW4345 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lhm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lhm RCSB], [http://www.ebi.ac.uk/pdbsum/4lhm PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lhm OCA], [http://pdbe.org/4lhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lhm RCSB], [http://www.ebi.ac.uk/pdbsum/4lhm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lhm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4lhm" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4lhm

From Proteopedia

Revision as of 09:47, 4 August 2016

Thymidine phosphorylase from E.coli with 3'-azido-3'-deoxythymidine

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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