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| | <StructureSection load='4xl3' size='340' side='right'caption='[[4xl3]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4xl3' size='340' side='right'caption='[[4xl3]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xl3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cloae Cloae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XL3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xl3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_acetobutylicum_EA_2018 Clostridium acetobutylicum EA 2018]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XL3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xl2|4xl2]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CEA_G2880 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=863638 CLOAE])</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=4xl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xl3 OCA], [https://pdbe.org/4xl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xl3 RCSB], [https://www.ebi.ac.uk/pdbsum/4xl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xl3 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </span></td></tr>
| + | |
| - | <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=4xl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xl3 OCA], [http://pdbe.org/4xl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xl3 RCSB], [http://www.ebi.ac.uk/pdbsum/4xl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xl3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0R4I970_CLOAE A0A0R4I970_CLOAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Thiolase|Thiolase]] | + | *[[Thiolase 3D structures|Thiolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cloae]] | + | [[Category: Clostridium acetobutylicum EA 2018]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylornithine carbamoyltransferase]]
| + | [[Category: Ahn JW]] |
| - | [[Category: Ahn, J W]] | + | [[Category: Ha SC]] |
| - | [[Category: Ha, S C]] | + | [[Category: Kim EJ]] |
| - | [[Category: Kim, E J]] | + | [[Category: Kim KJ]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim S]] |
| - | [[Category: Kim, S]] | + | [[Category: Lim JH]] |
| - | [[Category: Lim, J H]] | + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
A0A0R4I970_CLOAE
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum. Nat Commun. 2015 Sep 22;6:8410. doi: 10.1038/ncomms9410. PMID:26391388 doi:http://dx.doi.org/10.1038/ncomms9410
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