Ternary structure of Plasmodium vivax N-myristoyltransferase with myristoyl-CoA and inhibitor IMP-0001173

Bolling, C.; Mendez, A.; Taylor, S.; Makumire, S.; Reers, A.; Zigweid, R.; Subramanian, S.; Dranow, D.M.; Staker, B.; Edwards, T.E.; Tate, E.W.; Bell, A.S.; Myler, P.J.; Asojo, O.A.; Chakafana, G.

doi:10.1107/S2053230X24008604

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Comparison of human NMTs with PvNMT. (a) PvNMT (gray) shares structural topology with the two human NMTs HsNMT1 (yellow) and HsNMT2 (pink). Myr-CoA is shown in green sticks, while IMP-0001173 is shown in blue sticks. (b) An ENDScript surface plot of PvNMT, in the same orientation as in (a), shows that the residues closest to the Myr-CoA- and peptide-binding sites are highly conserved and form an interconnected cavity. Red regions represent higher conserved regions, while white represents regions with low conservation. Myr-CoA is shown in green sticks while IMP-0001173 is shown in blue sticks.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 80| Part 10| October 2024| Pages 269-277

https://doi.org/10.1107/S2053230X24008604

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