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| | <StructureSection load='3row' size='340' side='right'caption='[[3row]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='3row' size='340' side='right'caption='[[3row]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3row]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xance Xance]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ROW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3row]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ROW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH, XCC0212 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE])</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]] 1.8487Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3row FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3row OCA], [https://pdbe.org/3row PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3row RCSB], [https://www.ebi.ac.uk/pdbsum/3row PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3row ProSAT]</span></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=3row FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3row OCA], [https://pdbe.org/3row PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3row RCSB], [https://www.ebi.ac.uk/pdbsum/3row PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3row ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/OLEA_XANCP OLEA_XANCP] Involved in olefin biosynthesis (PubMed:21266575, PubMed:22524624, PubMed:27815501, PubMed:28223313). Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate (PubMed:21266575, PubMed:22524624, PubMed:27815501). Is active with fatty acyl-CoA substrates that ranged from C(8) to C(16) in length, and is the most active with palmitoyl-CoA and myristoyl-CoA (PubMed:21266575).<ref>PMID:21266575</ref> <ref>PMID:22524624</ref> <ref>PMID:27815501</ref> <ref>PMID:28223313</ref> |
| - | OleA is a thiolase superfamily enzyme which has been shown to catalyze the condensation of two long-chain fatty-acyl-Coenzyme A (CoA) substrates. The enzyme is part of a larger gene cluster responsible for generating long-chain olefin products - a potential biofuel precursor. In thiolase superfamily enzymes, catalysis is achieved via a ping-pong mechanism. The first substrate forms a covalent intermediate with an active site cysteine which is followed by reaction with the second substrate. For OleA, this conjugation proceeds by a non-decarboxylative Claisen condensation. The OleA from Xanthomonas campestris has been crystallized and its structure solved, along with inhibitor bound and xenon derivatized structures, to better understand substrate positioning in the context of enzyme turnover. OleA is the first characterized thiolase superfamily member that has two long-chain alkyl substrates that need to be bound simultaneously, and therefore uniquely requires an additional alkyl binding channel. The location of the fatty acid biosynthesis inhibitor, cerulenin, that possesses an alkyl chain length in the range of known OleA substrates, in conjunction with a single xenon binding site, leads to the putative assignment of this novel alkyl binding channel. Structural overlays between the OleA homologs, 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase and the fatty acid biosynthesis enzyme FabH, allow assignment of the remaining two channels; one for the thioester-containing pantetheinate arm and the second for the alkyl group of one substrate. A short beta-hairpin region is ordered in only one of the crystal forms and that may suggest open and closed states relevant for substrate binding. Cys143 is the conserved catalytic cysteine within the superfamily, and the site of alkylation by cerulenin. The alkylated structure suggests that a glutamic acid residue (Glu117beta) likely promotes Claisen condensation by acting as the catalytic base. Unexpectedly Glu117beta comes from the other monomer of the physiological dimer.
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| - | Crystal Structures of Xanthomonas Campestris OleA Reveal Features That Promote Head-to-Head Condensation of Two Long-Chain Fatty Acids.,Goblirsch BR, Frias JA, Wackett LP, Wilmot CM Biochemistry. 2012 Apr 23. PMID:22524624<ref>PMID:22524624</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 3row" style="background-color:#fffaf0;"></div> | + | |
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| | ==See Also== | | ==See Also== |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xance]] | + | [[Category: Xanthomonas campestris pv. campestris]] |
| - | [[Category: Goblirsch, B R]] | + | [[Category: Goblirsch BR]] |
| - | [[Category: Wilmot, C M]] | + | [[Category: Wilmot CM]] |
| - | [[Category: Non-decarboxylative claisen condensation]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
OLEA_XANCP Involved in olefin biosynthesis (PubMed:21266575, PubMed:22524624, PubMed:27815501, PubMed:28223313). Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate (PubMed:21266575, PubMed:22524624, PubMed:27815501). Is active with fatty acyl-CoA substrates that ranged from C(8) to C(16) in length, and is the most active with palmitoyl-CoA and myristoyl-CoA (PubMed:21266575).[1] [2] [3] [4]
See Also
References
- ↑ Frias JA, Richman JE, Erickson JS, Wackett LP. Purification and characterization of OleA from Xanthomonas campestris and demonstration of a non-decarboxylative Claisen condensation reaction. J Biol Chem. 2011 Apr 1;286(13):10930-8. doi: 10.1074/jbc.M110.216127. Epub 2011 , Jan 25. PMID:21266575 doi:http://dx.doi.org/10.1074/jbc.M110.216127
- ↑ Goblirsch BR, Frias JA, Wackett LP, Wilmot CM. Crystal Structures of Xanthomonas Campestris OleA Reveal Features That Promote Head-to-Head Condensation of Two Long-Chain Fatty Acids. Biochemistry. 2012 Apr 23. PMID:22524624 doi:10.1021/bi300386m
- ↑ Goblirsch BR, Jensen MR, Mohamed FA, Wackett LP, Wilmot CM. Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis. J Biol Chem. 2016 Dec 23;291(52):26698-26706. doi: 10.1074/jbc.M116.760892. Epub , 2016 Nov 4. PMID:27815501 doi:http://dx.doi.org/10.1074/jbc.M116.760892
- ↑ Christenson JK, Jensen MR, Goblirsch BR, Mohamed F, Zhang W, Wilmot CM, Wackett LP. Active Multienzyme Assemblies for Long-Chain Olefinic Hydrocarbon Biosynthesis. J Bacteriol. 2017 Apr 11;199(9):e00890-16. doi: 10.1128/JB.00890-16. Print 2017 , May 1. PMID:28223313 doi:http://dx.doi.org/10.1128/JB.00890-16
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