View source for 3sps


==Crystal Structure of Apo-Hexameric Acyl-CoA Thioesterase==
<StructureSection load='3sps' size='340' side='right'caption='[[3sps]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sps]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SPS 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]] 2.9&#8491;</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=3sps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sps OCA], [https://pdbe.org/3sps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sps RCSB], [https://www.ebi.ac.uk/pdbsum/3sps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sps ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9KEQ1_HALH5 Q9KEQ1_HALH5] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Acyl-coenzyme A (acyl-CoA) thioesterases play a crucial role in the metabolism of activated fatty acids, coenzyme A, and other metabolic precursor molecules including arachidonic acid and palmitic acid. These enzymes hydrolyze coenzyme A from acyl-CoA esters to mediate a range of cellular functions including beta-oxidation, lipid biosynthesis, and signal transduction. Here, we present the crystal structure of a hexameric hot-dog domain-containing acyl-CoA thioesterase from Bacillus halodurans in the apo-form and provide structural and comparative analyses to the coenzyme A-bound form to identify key conformational changes induced upon ligand binding. We observed dramatic ligand-induced changes at both the hot-dog dimer and the trimer-of-dimer interfaces; the dimer interfaces in the apo-structure differ by over 20% and decrease to about half the size in the ligand-bound state. We also assessed the specificity of the enzyme against a range of fatty acyl-CoA substrates and have identified a preference for short-chain fatty acyl-CoAs. Coenzyme A was shown both to negatively regulate enzyme activity, representing a direct inhibitory feedback, and consistent with the structural data, to destabilize the quaternary structure of the enzyme. Coenzyme A-induced conformational changes in the C-terminal helices of enzyme were assessed through mutational analysis and shown to play a role in regulating enzyme activity. The conformational changes are likely to be conserved from bacteria through to humans and provide a greater understanding, particularly at a structural level, of thioesterase function and regulation.

Ligand-induced conformational changes within a hexameric Acyl-CoA thioesterase.,Marfori M, Kobe B, Forwood JK J Biol Chem. 2011 Oct 14;286(41):35643-9. doi: 10.1074/jbc.M111.225953. Epub 2011, Aug 17. PMID:21849495<ref>PMID:21849495</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3sps" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alkalihalobacillus halodurans C-125]]
[[Category: Large Structures]]
[[Category: Forwood JK]]
[[Category: Kobe B]]
[[Category: Marfori M]]