9l4q
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the carbamoyl N-methyltransferase Asc-Orf2 complexed with SAH== | |
| + | <StructureSection load='9l4q' size='340' side='right'caption='[[9l4q]], [[Resolution|resolution]] 2.27Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9l4q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis Amycolatopsis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9L4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9L4Q 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]] 2.27Å</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=9l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9l4q OCA], [https://pdbe.org/9l4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9l4q RCSB], [https://www.ebi.ac.uk/pdbsum/9l4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9l4q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A229RJG8_AMYAL A0A229RJG8_AMYAL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Primary amide-specific N-methyltransferases are extremely scarce in microbial secondary metabolism. Here, Asc-Orf2, an N-methyltransferase involved in the biosynthesis of ansacarbamitocins, was identified to catalyze the methylation of the 3-O-carbamoyl moiety. Structural analysis identified an unprecedented NPPH catalytic motif, offering a mechanistic basis to overcome the chemical inertness of primary amides. The 3-O-(N-methyl)-carbamoyl maytansinoid derivatives, modified via Asc-Orf2-catalyzed methylation, exhibited markedly enhanced antitumor activity, highlighting the magic methylation effect in bioactivity modulation. Furthermore, structure-targeted engineering expanded the catalytic scope of Asc-Orf2, enabling the directed synthesis of an N-allylated carbamoyl maytansinoid derivative optimized for antibody-drug conjugate payload. | ||
| - | + | A Carbamoyl N-Methyltransferase Catalyzes N-Methylation of the Primary Amide in Ansacarbamitocin Biosynthesis.,Li Z, Yang W, Sun Z, Wang H, Lu C, Zhu D, Shen Y J Am Chem Soc. 2025 Jul 16;147(28):24186-24192. doi: 10.1021/jacs.5c05398. Epub , 2025 Jul 2. PMID:40601550<ref>PMID:40601550</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9l4q" style="background-color:#fffaf0;"></div> |
| - | [[Category: Li | + | == References == |
| - | [[Category: Zhu | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Amycolatopsis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Li ZY]] | ||
| + | [[Category: Shen YM]] | ||
| + | [[Category: Zhu DY]] | ||
Current revision
Crystal structure of the carbamoyl N-methyltransferase Asc-Orf2 complexed with SAH
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