9l4q | pdb_00009l4q

Crystal structure of the carbamoyl N-methyltransferase Asc-Orf2 complexed with SAH

spinqualitylabelsall models 9l4q, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9l4q is a 2 chain structure with sequence from Amycolatopsis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.27Å Ligands: SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A229RJG8_AMYAL 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA