Extended Data Fig. 8: Cis-peptide bond and metallic centers in Mmp10. | Nature

Extended Data Fig. 8: Cis-peptide bond and metallic centers in Mmp10.

From: Crystallographic snapshots of a B12-dependent radical SAM methyltransferase

Extended Data Fig. 8

a, Cis-peptide bonds at the interface between the radical SAM and the cobalamin binding domains in the substrate free (Mmp10 MTA_1 structure) and b, peptide-bound Mmp10 structures. Peptide substrate shown in orange with the radical SAM domain coloured in light blue and cobalamin binding domain in teal. Polar interactions shown as yellow staggered lines. Cis-peptide bond between T257 and P258 are coordinating a water molecule which is also involved in substrate binding. The rare non-proline cis-peptide bond found between L259 and E260 is held in place through interactions between the sidechain nitrogens of R243 and R298 and the side chain oxygens of E260. c, Metallic centres in Mmp10. Mmp10 SAM peptide structure. Peptide substrate shown in orange.

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