6b2t: Difference between revisions
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==Crystal structure of Xanthomonas campestris OleA H285D== | |||
<StructureSection load='6b2t' size='340' side='right' caption='[[6b2t]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6b2t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B2T 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=6b2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b2t OCA], [http://pdbe.org/6b2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b2t RCSB], [http://www.ebi.ac.uk/pdbsum/6b2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b2t 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 6b2t" 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]] | |||