5f2n
From Proteopedia
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| - | ''' | + | ==Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and 3-hydroxy-decanoate.== |
| + | <StructureSection load='5f2n' size='340' side='right' caption='[[5f2n]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5f2n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F2N FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5UF:(3~{S})-3-OXIDANYLDECANOIC+ACID'>5UF</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f2k|5f2k]], [[5f2o|5f2o]]</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=5f2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2n OCA], [http://pdbe.org/5f2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f2n RCSB], [http://www.ebi.ac.uk/pdbsum/5f2n PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transesterification of fatty acids yields the essential component of biodiesel, but current processes are cost-prohibitive and generate waste. Recent efforts make use of biocatalysts that are effective in diverting products from primary metabolism to yield fatty acid methyl esters in bacteria. These biotransformations require the fatty acid O-methyltransferase (FAMT) from Mycobacterium marinum (MmFAMT). Although this activity was first reported in the literature in 1970, the FAMTs have yet to be biochemically characterized. Here, we describe several crystal structures of MmFAMT, which highlight an unexpected structural conservation with methyltransferases that are involved in plant natural product metabolism. The determinants for ligand recognition are analyzed by kinetic analysis of structure-based active-site variants. These studies reveal how an architectural fold employed in plant natural product biosynthesis is used in bacterial fatty acid O-methylation. | ||
| - | + | Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel.,Petronikolou N, Nair SK Chem Biol. 2015 Nov 19;22(11):1480-90. doi: 10.1016/j.chembiol.2015.09.011. Epub , 2015 Oct 29. PMID:26526103<ref>PMID:26526103</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5f2n" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Nair, S K]] | ||
[[Category: Petronikolou, N]] | [[Category: Petronikolou, N]] | ||
| - | [[Category: | + | [[Category: 3-hydroxy-decanoate]] |
| + | [[Category: Fatty acid methyltransferase]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 19:30, 30 December 2015
Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and 3-hydroxy-decanoate.
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