3kvy
From Proteopedia
(Difference between revisions)
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<StructureSection load='3kvy' size='340' side='right'caption='[[3kvy]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3kvy' size='340' side='right'caption='[[3kvy]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3kvy]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3kvy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KVY FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=R2B:1,4-ANHYDRO-D-ERYTHRO-PENT-1-ENITOL'>R2B</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=R2B:1,4-ANHYDRO-D-ERYTHRO-PENT-1-ENITOL'>R2B</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=URA:URACIL'>URA</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=3kvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kvy OCA], [https://pdbe.org/3kvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kvy RCSB], [https://www.ebi.ac.uk/pdbsum/3kvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kvy ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A5PJH9_BOVIN A5PJH9_BOVIN] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=3kvy ConSurf]. | </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=3kvy ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Uridine phosphorylase is a key enzyme in the pyrimidine salvage pathway. This enzyme catalyzes the reversible phosphorolysis of uridine to uracil and ribose 1-phosphate (or 2'-deoxyuridine to 2'-deoxyribose 1-phosphate). Here we report the structure of hexameric Escherichia coli uridine phosphorylase treated with 5-fluorouridine and sulfate and dimeric bovine uridine phosphorylase treated with 5-fluoro-2'-deoxyuridine or uridine, plus sulfate. In each case the electron density shows three separate species corresponding to the pyrimidine base, sulfate, and a ribosyl species, which can be modeled as a glycal. In the structures of the glycal complexes, the fluorouracil O2 atom is appropriately positioned to act as the base required for glycal formation via deprotonation at C2'. Crystals of bovine uridine phosphorylase treated with 2'-deoxyuridine and sulfate show intact nucleoside. NMR time course studies demonstrate that uridine phosphorylase can catalyze the hydrolysis of the fluorinated nucleosides in the absence of phosphate or sulfate, without the release of intermediates or enzyme inactivation. These results add a previously unencountered mechanistic motif to the body of information on glycal formation by enzymes catalyzing the cleavage of glycosyl bonds. | ||
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- | Glycal formation in crystals of uridine phosphorylase.,Paul D, O'Leary SE, Rajashankar K, Bu W, Toms A, Settembre EC, Sanders JM, Begley TP, Ealick SE Biochemistry. 2010 Apr 27;49(16):3499-509. PMID:20364833<ref>PMID:20364833</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3kvy" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Uridine phosphorylase 3D structures|Uridine phosphorylase 3D structures]] | *[[Uridine phosphorylase 3D structures|Uridine phosphorylase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Bos taurus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Begley | + | [[Category: Begley TP]] |
- | [[Category: Bu | + | [[Category: Bu W]] |
- | [[Category: Ealick | + | [[Category: Ealick SE]] |
- | [[Category: Leary | + | [[Category: O'Leary S]] |
- | [[Category: Paul | + | [[Category: Paul D]] |
- | [[Category: Rajashankar | + | [[Category: Rajashankar K]] |
- | [[Category: Sanders | + | [[Category: Sanders J]] |
- | [[Category: Settembre | + | [[Category: Settembre E]] |
- | [[Category: Toms | + | [[Category: Toms A]] |
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Current revision
Trapping of an oxocarbenium ion intermediate in UP crystals
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Categories: Bos taurus | Large Structures | Begley TP | Bu W | Ealick SE | O'Leary S | Paul D | Rajashankar K | Sanders J | Settembre E | Toms A