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==Crystal structure of C212S mutant of Shewanella oneidensis MR-1 uridine phosphorylase==
<StructureSection load='4yjk' size='340' side='right'caption='[[4yjk]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yjk]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis_MR-1 Shewanella oneidensis MR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YJK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4yjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjk OCA], [https://pdbe.org/4yjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yjk RCSB], [https://www.ebi.ac.uk/pdbsum/4yjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yjk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8E9X9_SHEON Q8E9X9_SHEON] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Uridine phosphorylase (UP; EC 2.4.2.3), a key enzyme in the pyrimidine-salvage pathway, catalyzes the reversible phosphorolysis of uridine to uracil and ribose 1-phosphate. The structure of the C212S mutant of uridine phosphorylase from the facultatively aerobic Gram-negative gamma-proteobacterium Shewanella oneidensis MR-1 (SoUP) was determined at 1.68 A resolution. A comparison of the structures of the mutant and the wild-type enzyme showed that one dimer in the mutant hexamer differs from all other dimers in the mutant and wild-type SoUP (both in the free form and in complex with uridine). The key difference is the `maximum open' state of one of the subunits comprising this dimer, which has not been observed previously for uridine phosphorylases. Some conformational features of the SoUP dimer that provide access of the substrate into the active site are revealed. The binding of the substrate was shown to require the concerted action of two subunits of the dimer. The changes in the three-dimensional structure induced by the C212S mutation account for the lower affinity of the mutant for inorganic phosphate, while the affinity for uridine remains unchanged.

Concerted action of two subunits of the functional dimer of Shewanella oneidensis MR-1 uridine phosphorylase derived from a comparison of the C212S mutant and the wild-type enzyme.,Safonova TN, Mordkovich NN, Veiko VP, Okorokova NA, Manuvera VA, Dorovatovskii PV, Popov VO, Polyakov KM Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):203-10. doi:, 10.1107/S2059798315024353. Epub 2016 Jan 22. PMID:26894668<ref>PMID:26894668</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yjk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Uridine phosphorylase 3D structures|Uridine phosphorylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Shewanella oneidensis MR-1]]
[[Category: Dorovatovsky PV]]
[[Category: Manuvera VA]]
[[Category: Mordkovich NN]]
[[Category: Polyakov KM]]
[[Category: Popov VO]]
[[Category: Safonova TN]]
[[Category: Veiko VP]]