View source for 5log


==Crystal Structure of SafC from Myxococcus xanthus bound to SAM==
<StructureSection load='5log' size='340' side='right' caption='[[5log]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5log]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LDP:L-DOPAMINE'>LDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">safC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34 ATCC 25232])</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=5log FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5log OCA], [http://pdbe.org/5log PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5log RCSB], [http://www.ebi.ac.uk/pdbsum/5log PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5log ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Mg2+ -dependent catechol-O-methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol-O-methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis.

Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity.,Siegrist J, Netzer J, Mordhorst S, Karst L, Gerhardt S, Einsle O, Richter M, Andexer JN FEBS Lett. 2017 Jan;591(2):312-321. doi: 10.1002/1873-3468.12530. Epub 2017 Jan, 8. PMID:27990630<ref>PMID:27990630</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 25232]]
[[Category: Einsle, O]]
[[Category: Gerhardt, S]]
[[Category: Netzer, J]]
[[Category: O-methyl transferase]]
[[Category: Sam]]
[[Category: Transferase]]