View source for 7o4r


==Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme with Coenzyme A bound at the thiolase active sites and additional binding site (CoA(HAD/KAT))==
<StructureSection load='7o4r' size='340' side='right'caption='[[7o4r]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7o4r]] 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=7O4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O4R 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]] 2.79&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7o4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o4r OCA], [https://pdbe.org/7o4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o4r RCSB], [https://www.ebi.ac.uk/pdbsum/7o4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o4r ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O53872_MYCTU O53872_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Mycobacterium tuberculosis trifunctional enzyme (MtTFE) is an alpha2beta2 tetrameric enzyme. The alpha-chain harbors the 2E-enoyl-CoA hydratase (ECH) and 3S-hydroxyacyl-CoA dehydrogenase (HAD) activities and the beta-chain provides the 3-ketoacyl-CoA thiolase (KAT) activity. Enzyme kinetic data reported here show that medium and long chain enoyl-CoA molecules are preferred substrates for MtTFE. Modelling studies indicate how the linear medium and long acyl chains of these substrates can bind to each of the active sites. In addition, crystallographic binding studies have identified three new CoA binding sites which are different from the previously known CoA binding sites of the three TFE active sites. Structure comparisons provide new insights into the properties of ECH, HAD and KAT active sites of MtTFE. The interactions of the adenine moiety of CoA with loop-2 of the ECH active site cause a conformational change of this loop by which a competent ECH active site is formed. The NAD(+) binding domain (domain C) of the HAD part of MtTFE has only a few interactions with the rest of the complex and adopts a range of open conformations, whereas the A-domain of the ECH part is rigidly fixed with respect to the HAD part. Two loops, the CB1-CA1 region and the catalytic CB4-CB5 loop, near the thiolase active site and the thiolase dimer interface, have high B-factors. Structure comparisons suggest that a competent and stable thiolase dimer is formed only when complexed with the alpha-chains, highlighting the importance of the assembly for the proper functioning of the complex.

Substrate specificity and conformational flexibility properties of the Mycobacterium tuberculosis beta-oxidation trifunctional enzyme.,Dalwani S, Lampela O, Leprovost P, Schmitz W, Juffer AH, Wierenga RK, Venkatesan R J Struct Biol. 2021 Aug 8;213(3):107776. doi: 10.1016/j.jsb.2021.107776. PMID:34371166<ref>PMID:34371166</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7o4r" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Dalwani S]]
[[Category: Venkatesan R]]
[[Category: Wierenga RK]]