1pr5: Difference between revisions

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-{{Seed}}
-[[Image:1pr5.png|left|200px]]
-<!--
+==Escherichia coli Purine Nucleoside Phosphorylase Complexed with 7-deazaadenosine and Phosphate/Sulfate==
-The line below this paragraph, containing "STRUCTURE_1pr5", creates the "Structure Box" on the page.
+<StructureSection load='1pr5' size='340' side='right'caption='[[1pr5]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
--->
+<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>
-{{STRUCTURE_1pr5|  PDB=1pr5  |  SCENE=  }}
+<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>
+</table>
+== 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1pr5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pr5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Purine 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.
-===Escherichia coli Purine Nucleoside Phosphorylase Complexed with 7-deazaadenosine and Phosphate/Sulfate===
+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<ref>PMID:12937174</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1pr5" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_12937174}}, adds the Publication Abstract to the page
+*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 12937174 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12937174}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia coli O157:H7]]
-PR5 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli,_and_escherichia_coli_o157:h7 Escherichia coli, and escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PR5 OCA].
+[[Category: Large Structures]]
+[[Category: Allan PW]]
-==Reference==
+[[Category: Bennett EM]]
-<ref group="xtra">PMID:12937174</ref><references group="xtra"/>
+[[Category: Ealick SE]]
-[[Category: Escherichia coli, and escherichia coli o157:h7]]
+[[Category: Li C]]
-[[Category: Purine-nucleoside phosphorylase]]
+[[Category: Parker WB]]
-[[Category: Allan, P W.]]
-[[Category: Bennett, E M.]]
-[[Category: Ealick, S E.]]
-[[Category: Li, C.]]
-[[Category: Parker, W B.]]
-[[Category: Protein-nucleoside complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:48:49 2009''