5f2k

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==Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and octanoate==
==Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and octanoate==
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<StructureSection load='5f2k' size='340' side='right' caption='[[5f2k]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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<StructureSection load='5f2k' size='340' side='right'caption='[[5f2k]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5f2k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycmm Mycmm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F2K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5f2k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_marinum_M Mycobacterium marinum M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F2K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f2n|5f2n]], [[5f2o|5f2o]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMAR_3356 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216594 MYCMM])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5f2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2k OCA], [https://pdbe.org/5f2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f2k RCSB], [https://www.ebi.ac.uk/pdbsum/5f2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f2k ProSAT]</span></td></tr>
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<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=5f2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2k OCA], [http://pdbe.org/5f2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f2k RCSB], [http://www.ebi.ac.uk/pdbsum/5f2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f2k ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B2HHT4_MYCMM B2HHT4_MYCMM]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5f2k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mycmm]]
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[[Category: Large Structures]]
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[[Category: Nair, S K]]
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[[Category: Mycobacterium marinum M]]
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[[Category: Petronikolou, N]]
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[[Category: Nair SK]]
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[[Category: Fatty acid methyltransferase]]
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[[Category: Petronikolou N]]
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[[Category: Methyltransferase]]
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[[Category: Octanoate]]
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[[Category: Transferase]]
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Current revision

Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and octanoate

PDB ID 5f2k

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