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| | ==Crystal Structure of Trans-2-Enoyl-CoA Reductase from Treponema denticola== | | ==Crystal Structure of Trans-2-Enoyl-CoA Reductase from Treponema denticola== |
| - | <StructureSection load='4ggo' size='340' side='right' caption='[[4ggo]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4ggo' size='340' side='right'caption='[[4ggo]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ggo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Trede Trede]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GGO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ggo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_denticola_ATCC_35405 Treponema denticola ATCC 35405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GGO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ggp|4ggp]]</td></tr> | + | </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=4ggo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ggo OCA], [https://pdbe.org/4ggo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ggo RCSB], [https://www.ebi.ac.uk/pdbsum/4ggo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ggo ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Codon optimized trans-2-enoyl-CoA reductase, TDE_0597 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243275 TREDE])</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/Geissoschizine_dehydrogenase Geissoschizine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.36 1.3.1.36] </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=4ggo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ggo OCA], [http://pdbe.org/4ggo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ggo RCSB], [http://www.ebi.ac.uk/pdbsum/4ggo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ggo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Y597_TREDE Y597_TREDE]] Probable reductase (By similarity). | + | [https://www.uniprot.org/uniprot/FABV_TREDE FABV_TREDE] Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA. In vitro it can also use hexenoyl-CoA and dodecenoyl-CoA as substrates (PubMed:22906002).<ref>PMID:17382934</ref> <ref>PMID:22906002</ref> <ref>PMID:23050861</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Geissoschizine dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Trede]] | + | [[Category: Treponema denticola ATCC 35405]] |
| - | [[Category: Bond-Watts, B B]] | + | [[Category: Bond-Watts BB]] |
| - | [[Category: Chang, M C.Y]] | + | [[Category: Chang MCY]] |
| - | [[Category: Weeks, A M]] | + | [[Category: Weeks AM]] |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: Reductase]]
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| - | [[Category: Rossmann fold]]
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| Structural highlights
Function
FABV_TREDE Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA. In vitro it can also use hexenoyl-CoA and dodecenoyl-CoA as substrates (PubMed:22906002).[1] [2] [3]
Publication Abstract from PubMed
The production of fatty acids is an important cellular pathway for both cellular function and the development of engineered pathways for the synthesis of advanced biofuels. Despite the conserved reaction chemistry of various fatty acid synthase systems, the individual isozymes that catalyze these steps are quite diverse in their structural and biochemical features and are important for controlling differences at the cellular level. One of the key steps in the fatty acid elongation cycle is the enoyl-ACP (CoA) reductase function that drives the equilibrium forward toward chain extension. In this work, we report the structural and biochemical characterization of the trans-enoyl-CoA reductase from Treponema denticola (tdTer), which has been utilized for the engineering of synthetic biofuel pathways with an order of magnitude increase in product titers compared to those of pathways constructed with other enoyl-CoA reductase components. The crystal structure of tdTer was determined to 2.00 A resolution and shows that the Ter enzymes are distinct from members of the FabI, FabK, and FabL families but are highly similar to members of the FabV family. Further biochemical studies show that tdTer uses an ordered bi-bi mechanism initiated by binding of the NADH redox cofactor, which is consistent with the behavior of other enoyl-ACP (CoA) reductases. Mutagenesis of the substrate binding loop, characterization of enzyme activity with respect to crotonyl-CoA, hexenoyl-CoA, and dodecenoyl-CoA substrates, and product inhibition by lauroyl-CoA suggest that this region is important for controlling chain length specificity, with the major portal playing a more important role for longer chain length substrates.
Biochemical and Structural Characterization of the trans-Enoyl-CoA Reductase from Treponema denticola.,Bond-Watts BB, Weeks AM, Chang MC Biochemistry. 2012 Aug 20. PMID:22906002[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tucci S, Martin W. A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola. FEBS Lett. 2007 Apr 17;581(8):1561-6. doi: 10.1016/j.febslet.2007.03.013. Epub, 2007 Mar 15. PMID:17382934 doi:http://dx.doi.org/10.1016/j.febslet.2007.03.013
- ↑ Bond-Watts BB, Weeks AM, Chang MC. Biochemical and Structural Characterization of the trans-Enoyl-CoA Reductase from Treponema denticola. Biochemistry. 2012 Aug 20. PMID:22906002 doi:10.1021/bi300879n
- ↑ Hu K, Zhao M, Zhang T, Zha M, Zhong C, Jiang Y, Ding J. Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutulicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism. Biochem J. 2012 Oct 11. PMID:23050861 doi:10.1042/BJ20120871
- ↑ Bond-Watts BB, Weeks AM, Chang MC. Biochemical and Structural Characterization of the trans-Enoyl-CoA Reductase from Treponema denticola. Biochemistry. 2012 Aug 20. PMID:22906002 doi:10.1021/bi300879n
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