View source for 4xl2


==Crystal structure of oxidized form of thiolase from Clostridium acetobutylicum==
<StructureSection load='4xl2' size='340' side='right'caption='[[4xl2]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xl2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_acetobutylicum_ATCC_824 Clostridium acetobutylicum ATCC 824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XL2 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]] 1.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xl2 OCA], [https://pdbe.org/4xl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xl2 RCSB], [https://www.ebi.ac.uk/pdbsum/4xl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xl2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THLA_CLOAB THLA_CLOAB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thiolase is the first enzyme catalysing the condensation of two acetyl-coenzyme A (CoA) molecules to form acetoacetyl-CoA in a dedicated pathway towards the biosynthesis of n-butanol, an important solvent and biofuel. Here we elucidate the crystal structure of Clostridium acetobutylicum thiolase (CaTHL) in its reduced/oxidized states. CaTHL, unlike those from other aerobic bacteria such as Escherichia coli and Zoogloea ramegera, is regulated by the redox-switch modulation through reversible disulfide bond formation between two catalytic cysteine residues, Cys88 and Cys378. When CaTHL is overexpressed in wild-type C. acetobutylicum, butanol production is reduced due to the disturbance of acidogenic to solventogenic shift. The CaTHL(V77Q/N153Y/A286K) mutant, which is not able to form disulfide bonds, exhibits higher activity than wild-type CaTHL, and enhances butanol production upon overexpression. On the basis of these results, we suggest that CaTHL functions as a key enzyme in the regulation of the main metabolism of C. acetobutylicum through a redox-switch regulatory mechanism.

Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum.,Kim S, Jang YS, Ha SC, Ahn JW, Kim EJ, Hong Lim J, Cho C, Shin Ryu Y, Kuk Lee S, Lee SY, Kim KJ Nat Commun. 2015 Sep 22;6:8410. doi: 10.1038/ncomms9410. PMID:26391388<ref>PMID:26391388</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xl2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thiolase 3D structures|Thiolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium acetobutylicum ATCC 824]]
[[Category: Large Structures]]
[[Category: Ahn JW]]
[[Category: Ha SC]]
[[Category: Kim EJ]]
[[Category: Kim KJ]]
[[Category: Kim S]]
[[Category: Lim JH]]