View source for 4adm


==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 [http://en.wikipedia.org/wiki/Myctu Myctu]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ADM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4adl|4adl]], [[4apa|4apa]], [[4apb|4apb]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4adm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4adm OCA], [http://pdbe.org/4adm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4adm RCSB], [http://www.ebi.ac.uk/pdbsum/4adm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4adm ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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).

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>

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: Fumarate hydratase]]
[[Category: Myctu]]
[[Category: Alzari, P M]]
[[Category: Bellinzoni, M]]
[[Category: Cole, S]]
[[Category: Haouz, A]]
[[Category: Mechaly, A E]]
[[Category: Miras, I]]
[[Category: Shepard, W]]
[[Category: Weber, P]]
[[Category: Fumarase]]
[[Category: Lyase]]
[[Category: Tricarboxylic acid cycle]]