4xl4

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'''Unreleased structure'''
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==Crystal structure of thiolase from Clostridium acetobutylicum in complex with CoA==
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<StructureSection load='4xl4' size='340' side='right' caption='[[4xl4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xl4]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4n46 4n46]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XL4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XL4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xl2|4xl2]], [[4xl3|4xl3]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </span></td></tr>
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<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=4xl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xl4 OCA], [http://pdbe.org/4xl4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xl4 RCSB], [http://www.ebi.ac.uk/pdbsum/4xl4 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4xl4 is ON HOLD until Paper Publication
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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>
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Authors: Kim, S., Ha, S.C., Ahn, J.W., Kim, E.J., Lim, J.H., Kim, K.J.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of thiolase from Clostridium acetobutylicum in complex with CoA
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<div class="pdbe-citations 4xl4" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Lim, J.H]]
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<references/>
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[[Category: Kim, K.J]]
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__TOC__
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[[Category: Ahn, J.W]]
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</StructureSection>
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[[Category: Kim, E.J]]
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[[Category: Acetyl-CoA C-acetyltransferase]]
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[[Category: Ha, S.C]]
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[[Category: Ahn, J W]]
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[[Category: Ha, S C]]
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[[Category: Kim, E J]]
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[[Category: Kim, K J]]
[[Category: Kim, S]]
[[Category: Kim, S]]
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[[Category: Lim, J H]]
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[[Category: Transferase]]

Revision as of 13:40, 7 October 2015

Crystal structure of thiolase from Clostridium acetobutylicum in complex with CoA

4xl4, resolution 1.90Å

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