The structure of omphalotin A (OphA) reveals a complex catenane-like arrangement in which the peptide substrate is clamped with its amide nitrogen aligned for nucleophilic attack on the methyl group of SAM.
This 3D printed protein model of Omphalotin A (OphA) Monomer 1. This protein model set was designed to pair with the publication listed below matching Figure.1 and printed in full-color sandstone.
The dimer has a pseudo interlocking ring (catenane) arrangement. The first monomer of the two chain protein structure is colored to visualize the methyltransferase domain (orange), the clasp domain (green), and C-terminal substrate peptide (cyan). The active site of OphA and the ligand S-Adenosylmethionne (SAM) are colored by their atom type. (carbon = orange/yellow, nitrogen = blue and oxygen = red.)
The second chain of the dimer colors the same regions in different colors. The other monomer is colored pink (N-terminal methyltransferase domain) and gray (C-terminal clasp domain). The clasp terminal domain wraps around the loops that cover the active site of the other monomer.
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Created from PDB ID: 5N0S