1loq: Difference between revisions

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-[[Image:1loq.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1loq", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1loq|  PDB=1loq  |  SCENE=  }}
-'''Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP'''
+==Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP==
+<StructureSection load='1loq' size='340' side='right'caption='[[1loq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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=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>
+</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/1loq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1loq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Overview==
+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:12011084<ref>PMID:12011084</ref>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-LOQ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOQ OCA].
+</div>
+<div class="pdbe-citations 1loq" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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://www.ncbi.nlm.nih.gov/pubmed/12011084 12011084]
+*[[Uridine 5'-monophosphate synthase 3D structures|Uridine 5'-monophosphate synthase 3D structures]]
-[[Category: Orotidine-5'-phosphate decarboxylase]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Pai, E F.]]
+__TOC__
-[[Category: Wu, N.]]
+</StructureSection>
-[[Category: Tim barrel]]
+[[Category: Archaea]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:07:36 2008''
+[[Category: Large Structures]]
+[[Category: Pai EF]]
+[[Category: Wu N]]