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2c5q
From Proteopedia
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| - | [[Image:2c5q.gif|left|200px]]<br /><applet load="2c5q" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2c5q, resolution 1.70Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF YEAST YER010CP'''<br /> | ||
| - | == | + | ==Crystal structure of yeast YER010Cp== |
| - | + | <StructureSection load='2c5q' size='340' side='right'caption='[[2c5q]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | [ | + | <table><tr><td colspan='2'>[[2c5q]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C5Q 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]] 1.7Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=2c5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5q OCA], [https://pdbe.org/2c5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c5q RCSB], [https://www.ebi.ac.uk/pdbsum/2c5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5q ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/RRAAH_YEAST RRAAH_YEAST] Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.<ref>PMID:24359411</ref> | |
| - | [ | + | == 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/c5/2c5q_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=2c5q ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We present here the structure of Yer010c protein of unknown function, solved by Multiple Anomalous Diffraction and revealing a common fold and oligomerization state with proteins of the regulator of ribonuclease activity A (RraA) family. In Escherichia coli, RraA has been shown to regulate the activity of ribonuclease E by direct interaction. The absence of ribonuclease E in yeast suggests a different function for this family member in this organism. Yer010cp has a few supplementary secondary structure elements and a deep pseudo-knot at the heart of the protein core. A tunnel at the interface between two monomers, lined with conserved charged residues, has unassigned residual electron density and may constitute an active site for a yet unknown activity. | ||
| - | + | Crystal structure of yeast YER010Cp, a knotable member of the RraA protein family.,Leulliot N, Quevillon-Cheruel S, Graille M, Schiltz M, Blondeau K, Janin J, Van Tilbeurgh H Protein Sci. 2005 Oct;14(10):2751-8. PMID:16195557<ref>PMID:16195557</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2c5q" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Blondeau K]] | ||
| + | [[Category: Graille M]] | ||
| + | [[Category: Janin J]] | ||
| + | [[Category: Leulliot N]] | ||
| + | [[Category: Quevillon-Cheruel S]] | ||
| + | [[Category: Schiltz M]] | ||
| + | [[Category: Van Tilbeurgh H]] | ||
Current revision
Crystal structure of yeast YER010Cp
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