View source for 22ow


==Crystal structure of O-adenosylmethionine-dependent methyltransferase McbD in complex with SAH==
<StructureSection load='22ow' size='340' side='right'caption='[[22ow]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[22ow]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinactinospora_thermotolerans Marinactinospora thermotolerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22OW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22OW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=22ow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22ow OCA], [https://pdbe.org/22ow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22ow RCSB], [https://www.ebi.ac.uk/pdbsum/22ow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22ow ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
O-Methylation represents a prevalent tailoring modification in natural product biosynthesis, significantly altering molecular properties and bioactivity. In this study, we report the crystal structure of the O-methyltransferase (MTase) McbD in complex with S-adenosyl-l-homocysteine (SAH) at 3.0 A resolution, complemented by a modeled binding pose for the substrate marinacarboline B (1). Through integrated site-directed mutagenesis and enzymatic assays, we identified critical residues required for catalytic activity and propose a refined mechanistic model for methyl transfer. These findings offer substantive structural and mechanistic insights into how O-MTases drive the diversification of bioactive natural products.

Structural and Mechanistic Insights into the OâMethyltransferase McbD in Marinacarboline Biosynthesis.,Qiao Z, Yang X, Liu J, Liu L, Meng X, He X, Liu G, Teng YB, Chen Q ACS Omega. 2026 Jun 1;11(23):34350-34356. doi: 10.1021/acsomega.6c02087. , eCollection 2026 Jun 16. PMID:42326699<ref>PMID:42326699</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 22ow" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Marinactinospora thermotolerans]]
[[Category: Qiao Z]]
[[Category: Teng YB]]