4adm: Difference between revisions

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-'''Unreleased structure'''
-The entry 4adm is ON HOLD
+==Crystal structure of Rv1098c in complex with meso-tartrate==
+<StructureSection load='4adm' size='340' side='right'caption='[[4adm]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4adm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ADM 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]] 1.65&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</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=4adm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4adm OCA], [https://pdbe.org/4adm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4adm RCSB], [https://www.ebi.ac.uk/pdbsum/4adm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4adm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FUMC_MYCTU FUMC_MYCTU] Catalyzes the reversible addition of water to fumarate to give L-malate.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+rv1098c, an essential gene in Mycobacterium tuberculosis, codes for a class II fumarase. We describe here the crystal structure of Rv1098c in complex with l-malate, fumarate or the competitive inhibitor meso-tartrate. The models reveal that substrate binding promotes the closure of the active site through conformational changes involving the catalytic SS-loop and the C-terminal domain, which likely represents a general feature of this enzyme superfamily. Analysis of ligand-enzyme interactions as well as site-directed mutagenesis suggest Ser318 as one of the two acid-base catalysts. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: Rv1098c and Rv1098c bind by X-ray crystallography (View interaction).
-Authors: Mechaly, A.E., Haouz, A., Miras, I., Weber, P., Shepard, W., Cole, S., Alzari, P.M., Bellinzoni, M.
+Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from Mycobacterium tuberculosis.,Mechaly AE, Haouz A, Miras I, Barilone N, Weber P, Shepard W, Alzari PM, Bellinzoni M FEBS Lett. 2012 Jun 4;586(11):1606-11. Epub 2012 May 3. PMID:22561013<ref>PMID:22561013</ref>
-Description: Crystal structure of Rv1098c in complex with meso-tartrate
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4adm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Fumarase|Fumarase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
+[[Category: Alzari PM]]
+[[Category: Bellinzoni M]]
+[[Category: Cole S]]
+[[Category: Haouz A]]
+[[Category: Mechaly AE]]
+[[Category: Miras I]]
+[[Category: Shepard W]]
+[[Category: Weber P]]