22ow: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
Line 1: Line 1:
'''Unreleased structure'''


The entry 22ow is ON HOLD  until Paper Publication
==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>
<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.


Authors: Qiao, Z., Teng, Y.B.
Structural and Mechanistic Insights into the O‑Methyltransferase 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>


Description: Crystal structure of O-adenosylmethionine-dependent methyltransferase McbD in complex with SAH
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Teng, Y.B]]
<div class="pdbe-citations 22ow" style="background-color:#fffaf0;"></div>
[[Category: Qiao, Z]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Marinactinospora thermotolerans]]
[[Category: Qiao Z]]
[[Category: Teng YB]]
Retrieved from "https://proteopedia.org/22ow"