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| | ==Crystal structure of Xanthomonas campestris OleA H285N== | | ==Crystal structure of Xanthomonas campestris OleA H285N== |
| - | <StructureSection load='6b2s' size='340' side='right' caption='[[6b2s]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='6b2s' size='340' side='right'caption='[[6b2s]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6b2s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B2S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6b2s]] 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=6B2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B2S 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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </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=6b2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b2s OCA], [https://pdbe.org/6b2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b2s RCSB], [https://www.ebi.ac.uk/pdbsum/6b2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b2s ProSAT]</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=6b2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b2s OCA], [http://pdbe.org/6b2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b2s RCSB], [http://www.ebi.ac.uk/pdbsum/6b2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b2s 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 6b2s" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6b2s" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Christenson, J K]] | + | [[Category: Large Structures]] |
| - | [[Category: Esler, M A]] | + | [[Category: Xanthomonas campestris pv. campestris str. ATCC 33913]] |
| - | [[Category: Goblirsch, B R]] | + | [[Category: Christenson JK]] |
| - | [[Category: Jensen, M R]] | + | [[Category: Esler MA]] |
| - | [[Category: Mohamed, F A]] | + | [[Category: Goblirsch BR]] |
| - | [[Category: Wackett, L P]] | + | [[Category: Jensen MR]] |
| - | [[Category: Wilmot, C M]] | + | [[Category: Mohamed FA]] |
| - | [[Category: Condensation]] | + | [[Category: Wackett LP]] |
| - | [[Category: Olea]] | + | [[Category: Wilmot CM]] |
| - | [[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
Renewable production of hydrocarbons is being pursued as a petroleum-independent source of commodity chemicals and replacement for biofuels. The bacterial biosynthesis of long-chain olefins represents one such platform. The process is initiated by OleA catalyzing the condensation of two fatty acyl-coenzyme A substrates to form a beta-keto acid. Here, the mechanistic role of the conserved His285 is investigated through mutagenesis, activity assays, and X-ray crystallography. Our data demonstrate that His285 is required for product formation, influences the thiolase nucleophile Cys143 and the acyl-enzyme intermediate before and after transesterification, and orchestrates substrate coordination as a defining component of an oxyanion hole. As a consequence, His285 plays a key role in enabling a mechanistic strategy in OleA that is distinct from other thiolases.
The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates.,Jensen MR, Goblirsch BR, Esler MA, Christenson JK, Mohamed FA, Wackett LP, Wilmot CM FEBS Lett. 2018 Feb 11. doi: 10.1002/1873-3468.13004. PMID:29430657[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
- ↑ Jensen MR, Goblirsch BR, Esler MA, Christenson JK, Mohamed FA, Wackett LP, Wilmot CM. The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates. FEBS Lett. 2018 Feb 11. doi: 10.1002/1873-3468.13004. PMID:29430657 doi:http://dx.doi.org/10.1002/1873-3468.13004
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