22ow: Difference between revisions
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==Crystal structure of O-adenosylmethionine-dependent methyltransferase McbD in complex with SAH== | |||
<StructureSection load='22ow' size='340' side='right'caption='[[22ow]], [[Resolution|resolution]] 3.00Å' 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]] 3Å</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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 22ow" style="background-color:#fffaf0;"></div> | ||
[[Category: Qiao | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Marinactinospora thermotolerans]] | |||
[[Category: Qiao Z]] | |||
[[Category: Teng YB]] | |||
Latest revision as of 07:17, 8 July 2026
Crystal structure of O-adenosylmethionine-dependent methyltransferase McbD in complex with SAH
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