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| | <StructureSection load='4kti' size='340' side='right'caption='[[4kti]], [[Resolution|resolution]] 1.84Å' scene=''> | | <StructureSection load='4kti' size='340' side='right'caption='[[4kti]], [[Resolution|resolution]] 1.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kti]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Xancp Xancp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KTI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kti]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris_str._ATCC_33913 Xanthomonas campestris pv. campestris str. ATCC 33913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KTI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3row|3row]], [[3s21|3s21]], [[3s23|3s23]], [[4ktm|4ktm]]</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=4kti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kti OCA], [https://pdbe.org/4kti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kti RCSB], [https://www.ebi.ac.uk/pdbsum/4kti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kti ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH, XCC0212 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190485 XANCP])</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=4kti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kti OCA], [http://pdbe.org/4kti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kti RCSB], [http://www.ebi.ac.uk/pdbsum/4kti PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kti ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4kti" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4kti" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xancp]] | + | [[Category: Xanthomonas campestris pv. campestris str. ATCC 33913]] |
| - | [[Category: Goblirsch, B R]] | + | [[Category: Goblirsch BR]] |
| - | [[Category: Thiolase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| 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]
Publication Abstract from PubMed
Phylogenetically diverse microbes that produce long chain, olefinic hydrocarbons have received much attention as possible sources of renewable energy biocatalysts. One enzyme that is critical for this process is OleA, a thiolase superfamily enzyme that condenses two fatty acyl-CoA substrates to produce a beta-ketoacid product and initiates the biosynthesis of long chain olefins in bacteria. Thiolases typically utilize a ping-pong mechanism centered on an active site cysteine residue. Reaction with the first substrate produces a covalent cysteine-thioester tethered acyl group that is transferred to the second substrate through formation of a carbon-carbon bond. Although the basics of thiolase chemistry are precedented, the mechanism by which OleA accommodates two substrates with extended carbon chains and a coenzyme moiety-unusual for a thiolase-are unknown. Gaining insights into this process could enable manipulation of the system for large scale olefin production with hydrocarbon chains lengths equivalent to those of fossil fuels. In this study, mutagenesis of the active site cysteine in Xanthomonas campestris OleA (Cys143) enabled trapping of two catalytically relevant species in crystals. In the resulting structures, long chain alkyl groups (C12 and C14) and phosphopantetheinate define three substrate channels in a T-shaped configuration, explaining how OleA coordinates its two substrates and product. The C143A OleA co-crystal structure possesses a single bound acyl-CoA representing the Michaelis complex with the first substrate, whereas the C143S co-crystal structure contains both acyl-CoA and fatty acid, defining how a second substrate binds to the acyl-enzyme intermediate. An active site glutamate (Glubeta117) is positioned to deprotonate bound acyl-CoA and initiate carbon-carbon bond formation.
Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis.,Goblirsch BR, Jensen MR, Mohamed FA, Wackett LP, Wilmot CM J Biol Chem. 2016 Dec 23;291(52):26698-26706. doi: 10.1074/jbc.M116.760892. Epub , 2016 Nov 4. PMID:27815501[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ 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
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