Structure of Plasmodium vivax N-myristoyltransferase with inhibitor IMP-1088: exploring an NMT inhibitor for antimalarial therapy

Mendez, A.; Bolling, C.; Taylor, S.; Makumire, S.; Staker, B.; Reers, A.; Hammerson, B.; Mayclin, S.J.; Abendroth, J.; Lorimer, D.D.; Edwards, T.E.; Tate, E.W.; Subramanian, S.; Bell, A.S.; Myler, P.J.; Asojo, O.A.; Chakafana, G.

doi:10.1107/S2053230X24011348

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
(a) The alignment shows residue conservation between NMTs from different organisms. Residues within the cofactor-binding pocket are shown in purple, while those in the substrate-binding pocket are shown in green. The secondary-structure alignment is based on our reported structure. (b) The residues located in the C-termini of different NMTs. The following NMTs are included in the alignment: PvNMT, P. falciparum NMT, HsNMT1, HsNMT2, Saccharomyces cerevisiae NMT, Candida albicans NMT, Aspergillus fumigatus NMT, A. flavus NMT, Leishmania major NMT, L. donovani NMT and Cryptosporidium parvum NMT.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 81| Part 1| January 2025|

https://doi.org/10.1107/S2053230X24011348

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