1pr6

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[[Image:1pr6.jpg|left|200px]]
 
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==Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-xylofuranosyladenine and Phosphate/Sulfate==
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The line below this paragraph, containing "STRUCTURE_1pr6", creates the "Structure Box" on the page.
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<StructureSection load='1pr6' size='340' side='right'caption='[[1pr6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1pr6]] 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=1PR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PR6 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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=XYA:2-(6-AMINO-OCTAHYDRO-PURIN-9-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>XYA</scene></td></tr>
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{{STRUCTURE_1pr6| PDB=1pr6 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pr6 OCA], [https://pdbe.org/1pr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1pr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pr6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEOD_ECO57 DEOD_ECO57] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1pr6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1pr6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-xylofuranosyladenine and Phosphate/Sulfate'''
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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>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1PR6 is a [[Single protein]] structure of sequence 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=1PR6 OCA].
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</div>
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<div class="pdbe-citations 1pr6" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12937174 12937174]
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*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
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[[Category: Escherichia coli, and escherichia coli o157:h7]]
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*[[Ribozyme 3D structures|Ribozyme 3D structures]]
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[[Category: Purine-nucleoside phosphorylase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Allan, P W.]]
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__TOC__
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[[Category: Bennett, E M.]]
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</StructureSection>
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[[Category: Ealick, S E.]]
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[[Category: Escherichia coli O157:H7]]
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[[Category: Li, C.]]
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[[Category: Large Structures]]
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[[Category: Parker, W B.]]
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[[Category: Allan PW]]
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[[Category: Protein-nucleoside complex]]
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[[Category: Bennett EM]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:23:55 2008''
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[[Category: Ealick SE]]
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[[Category: Li C]]
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[[Category: Parker WB]]

Current revision

Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-xylofuranosyladenine and Phosphate/Sulfate

PDB ID 1pr6

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