9wiv: Difference between revisions
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==SbSOMT in complex with SAH== | |||
<StructureSection load='9wiv' size='340' side='right'caption='[[9wiv]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9wiv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorghum_bicolor Sorghum bicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9WIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WIV 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]] 2.9Å</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=9wiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wiv OCA], [https://pdbe.org/9wiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wiv RCSB], [https://www.ebi.ac.uk/pdbsum/9wiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wiv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1B6PFV1_SORBI A0A1B6PFV1_SORBI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SAM-dependent methyltransferases are enzymes that catalyze the transfer of a methyl group from a cofactor to a substrate through an ordered or random sequential bi-bi mechanism. However, the structural dynamics governing binding cooperativity between the cofactor and substrate remain understudied. In this study, we demonstrate that SbSOMT, a plant O-methyltransferase, exhibits bilateral positive cooperativity between the cofactor and substrate, except the unproductive SbSOMT-SAM-pterostilbene complex. Furthermore, SbSOMT displayed substrate-binding kinetics that shift in response to the nature of bound-cofactor. Sinefungin-bound SbSOMT exhibited positive cooperativity primarily attributed to an increased substrate association rate constant (k(on)), whereas SAH-bound SbSOMT displayed positive cooperativity driven primarily by a decreased dissociation rate constant (k(off)). Structural analysis implies that these cooperativity switch and divergent binding kinetics stem from the interactions between the cofactor and substrate at the methyl binding site. Integrating structural insights reveals that a dynamic W279 pi-stacking network governs this cooperativity. Upon binding of the first ligand, H196, W279, and H282 rearrange to form a pi-stacking network, in which W279 serves as the essential central plane that also stacks with the substrate. Accordingly, W279A mutagenesis substantially impaired the substrate affinity, cooperativity and enzymatic activity. | |||
Structural dynamics of the pi-stacking network governing cofactor-substrate cooperativity of SbSOMT methyltransferase.,Pow KC, Zhang N, Yan M, Wang X, Lui ACW, Lo C, Hao Q Commun Chem. 2026 Jun 8. doi: 10.1038/s42004-026-02087-3. PMID:42259925<ref>PMID:42259925</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hao | <div class="pdbe-citations 9wiv" style="background-color:#fffaf0;"></div> | ||
[[Category: Pow | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sorghum bicolor]] | |||
[[Category: Hao Q]] | |||
[[Category: Pow KC]] | |||
