4apb: Difference between revisions
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< | ==Crystal structure of Mycobacterium tuberculosis fumarase (Rv1098c) S318C in complex with fumarate== | ||
<StructureSection load='4apb' size='340' side='right'caption='[[4apb]], [[Resolution|resolution]] 1.94Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4apb]] 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=4APB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4APB 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]] 1.94Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</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=4apb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apb OCA], [https://pdbe.org/4apb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4apb RCSB], [https://www.ebi.ac.uk/pdbsum/4apb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4apb 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). | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4apb" 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: Haouz A]] | ||
[[Category: | [[Category: Mechaly AE]] | ||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Alzari | |||
[[Category: Bellinzoni | |||
[[Category: Haouz | |||
[[Category: Mechaly | |||
Latest revision as of 12:10, 15 November 2023
Crystal structure of Mycobacterium tuberculosis fumarase (Rv1098c) S318C in complex with fumarateCrystal structure of Mycobacterium tuberculosis fumarase (Rv1098c) S318C in complex with fumarate
Structural highlights
FunctionFUMC_MYCTU Catalyzes the reversible addition of water to fumarate to give L-malate. Publication Abstract from PubMedrv1098c, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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