6b2s
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Xanthomonas campestris OleA H285N== | |
| + | <StructureSection load='6b2s' size='340' side='right' caption='[[6b2s]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == 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> | ||
| + | </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> | ||
| + | <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='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'>[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:29430657</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6b2s" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Mohamed, F | + | <references/> |
| - | [[Category: Wackett, L | + | __TOC__ |
| - | [[Category: Wilmot, C | + | </StructureSection> |
| - | [[Category: | + | [[Category: Christenson, J K]] |
| - | [[Category: | + | [[Category: Esler, M A]] |
| + | [[Category: Goblirsch, B R]] | ||
| + | [[Category: Jensen, M R]] | ||
| + | [[Category: Mohamed, F A]] | ||
| + | [[Category: Wackett, L P]] | ||
| + | [[Category: Wilmot, C M]] | ||
| + | [[Category: Condensation]] | ||
| + | [[Category: Olea]] | ||
| + | [[Category: Thiolase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:30, 28 February 2018
Crystal structure of Xanthomonas campestris OleA H285N
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