1pr5: Difference between revisions
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<StructureSection load='1pr5' size='340' side='right'caption='[[1pr5]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1pr5' size='340' side='right'caption='[[1pr5]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pr5]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1pr5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PR5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TBN:2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>TBN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pr5 OCA], [https://pdbe.org/1pr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pr5 RCSB], [https://www.ebi.ac.uk/pdbsum/1pr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pr5 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DEOD_ECO57 DEOD_ECO57] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli | [[Category: Escherichia coli O157:H7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Allan PW]] | |||
[[Category: Allan | [[Category: Bennett EM]] | ||
[[Category: Bennett | [[Category: Ealick SE]] | ||
[[Category: Ealick | [[Category: Li C]] | ||
[[Category: Li | [[Category: Parker WB]] | ||
[[Category: Parker | |||
Latest revision as of 12:46, 16 August 2023
Escherichia coli Purine Nucleoside Phosphorylase Complexed with 7-deazaadenosine and Phosphate/SulfateEscherichia coli Purine Nucleoside Phosphorylase Complexed with 7-deazaadenosine and Phosphate/Sulfate
Structural highlights
FunctionDEOD_ECO57 Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPurine nucleoside phosphorylase catalyzes reversible phosphorolysis of purine nucleosides and 2'-deoxypurine nucleosides to the free base and ribose (or 2'-deoxyribose) 1-phosphate. Whereas the human enzyme is specific for 6-oxopurine ribonucleosides, the Escherichia coli enzyme accepts additional substrates including 6-oxopurine ribonucleosides, 6-aminopurine ribonucleosides, and to a lesser extent purine arabinosides. These differences have been exploited in a potential suicide gene therapy treatment for solid tumors. In an effort to optimize this suicide gene therapy approach, we have determined the three-dimensional structure of the E. coli enzyme in complex with 10 nucleoside analogs and correlated the structures with kinetic measurements and computer modeling. These studies explain the preference of the enzyme for ribose sugars, show increased flexibility for active site residues Asp204 and Arg24, and suggest that interactions involving the 1- and 6-positions of the purine and the 4'- and 5'-positions of the ribose provide the best opportunities to increase prodrug specificity and enzyme efficiency. Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase.,Bennett EM, Li C, Allan PW, Parker WB, Ealick SE J Biol Chem. 2003 Nov 21;278(47):47110-8. Epub 2003 Aug 21. PMID:12937174[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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