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1loq

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(New page: 200px<br /><applet load="1loq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1loq, resolution 1.50&Aring;" /> '''Crystal structure of...)
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[[Image:1loq.jpg|left|200px]]<br /><applet load="1loq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1loq, resolution 1.50&Aring;" />
 
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'''Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP'''<br />
 
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==Overview==
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==Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP==
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The crystal structures of the enzyme orotidine-5'-monophosphate, decarboxylase from Methanobacterium thermoautotrophicum complexed with its, product UMP and the inhibitors 6-hydroxyuridine 5'-phosphate (BMP), XMP, and CMP are reported. A mutant version of the protein, in which four, residues of the flexible phosphate-binding loop (180)Gly-Gly(190) were, removed and Arg(203) was replaced by alanine, was also analyzed. The XMP, and CMP complexes reveal a ligand-binding mode that is distinct from the, one identified previously with the aromatic rings located outside the, binding pocket. A potential pathway for ligand binding is discussed.
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<StructureSection load='1loq' size='340' side='right'caption='[[1loq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1loq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaea Archaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LOQ FirstGlance]. <br>
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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]] 1.5&#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=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
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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=1loq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1loq OCA], [https://pdbe.org/1loq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1loq RCSB], [https://www.ebi.ac.uk/pdbsum/1loq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1loq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRF_METTH PYRF_METTH] Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).[HAMAP-Rule:MF_01200_A]
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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/lo/1loq_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=1loq ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LOQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with U as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LOQ OCA].
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*[[Uridine 5'-monophosphate synthase 3D structures|Uridine 5'-monophosphate synthase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase., Wu N, Pai EF, J Biol Chem. 2002 Aug 2;277(31):28080-7. Epub 2002 May 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12011084 12011084]
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[[Category: Archaea]]
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[[Category: ]]
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[[Category: Large Structures]]
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[[Category: Orotidine-5'-phosphate decarboxylase]]
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[[Category: Pai EF]]
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[[Category: Single protein]]
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[[Category: Wu N]]
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[[Category: Pai, E.F.]]
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[[Category: Wu, N.]]
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[[Category: U]]
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[[Category: tim barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:44:02 2007''
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Current revision

Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP

PDB ID 1loq

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