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Figure 1
Ternary structure of PvNMT with Myr-CoA and the inhibitor IMP-1088. (a) There are three PvNMT monomers in the asymmetric unit: A (marine), B (gray) and C (light brown). Each has a bound Myr-CoA (magenta) and IMP-1088 inhibitor (green). (b) Superposed monomers are almost identical, with an r.m.s.d. of ∼0.10 Å on Cα atoms. Each monomer is colored in a rainbow from blue at the N-terminus to red at the C-terminus. Myr-CoA is shown as magenta sticks, while the inhibitor IMP-1088 is shown as green sticks. (c) Superposed monomers of PvNMT (PDB entry 5v0w, gray), HsNMT1 (PDB entry 5mu6, pink) and HsNMT2 (PDB entry 4c2x, cyan). Myr-CoA is shown as magenta sticks, while the inhibitor IMP-1088 is shown as green sticks. (d) Solvent-accessible surface area of PvNMT colored by sequence conservation, with red indicating identical residues. The peptide/substrate-binding and myristoyl-binding cavities are shown in black parentheses.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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