22ow

Crystal structure of O-adenosylmethionine-dependent methyltransferase McbD in complex with SAH

spinqualitylabelsall models 22ow, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 22ow is a 2 chain structure with sequence from Marinactinospora thermotolerans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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