Crystal structure and functional characterization of an Asp49 phospholipase A2 from the bushmaster (Lachesis muta)

Neyra Chama, N.E.; Romero Vargas, F.F.; Condori Mamani, E.; Vargas, J.A.; Alves Furtado, A.; D'Muniz Pereira, H.; Navarro Oviedo, R.D.; Garratt, R.C.; Vega Ramírez, J.L.J.; Leonardo, D.A.

doi:10.1107/S2053230X26002736

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 6
Structural comparison of dimeric conformations in snake-venom PLA₂ enzymes. (a) Dimer formed by chains A and A′ in the L. muta Asp49-PLA₂ PISA assembly compared with the conventional and compact dimers of BthTX-II (PDB entry 2oqd; red and blue, respectively). Superpositions yielded r.m.s.d. values of 14.2 Å (conventional) and 7.8 Å (compact). (b) Comparison of the L. muta Asp49-PLA₂ dimer (green) with the CBd isoform from C. durissus terrificus (PDB entrty 6tmy), showing an r.m.s.d. of 3.6 Å.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 82| Part 5| May 2026| Pages 150-159

https://doi.org/10.1107/S2053230X26002736

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