1los: Difference between revisions

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OCA

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-[[Image:1los.gif|left|200px]]<br /><applet load="1los" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1los, resolution 1.90&Aring;" />
-'''crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP'''<br />
-==Overview==
+==crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP==
-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.
+<StructureSection load='1los' size='340' side='right'caption='[[1los]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1los]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LOS 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UP6:6-AZA+URIDINE+5-MONOPHOSPHATE'>UP6</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=1los FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1los OCA], [https://pdbe.org/1los PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1los RCSB], [https://www.ebi.ac.uk/pdbsum/1los PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1los ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]
+== 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/lo/1los_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=1los ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-LOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with UP6 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=1LOS OCA].
+*[[Uridine 5'-monophosphate synthase 3D structures|Uridine 5'-monophosphate synthase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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]
+[[Category: Large Structures]]
-[[Category: Methanothermobacter thermautotrophicus]]
+[[Category: Methanothermobacter thermautotrophicus str. Delta H]]
-[[Category: Orotidine-5'-phosphate decarboxylase]]
+[[Category: Pai EF]]
-[[Category: Single protein]]
+[[Category: Wu N]]
-[[Category: Pai, E.F.]]
-[[Category: Wu, N.]]
-[[Category: UP6]]
-[[Category: tim barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:44:10 2007''