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Figure 4
Sequence and structural comparison of the β-hairpin region in snake-venom PLA2s. (a) Multiple sequence alignment of PLA2 enzymes from group I (elapid) and group II (viperid) snakes. Residues involved in calcium binding and the catalytic dyad are highlighted. Cysteines required for the β-hairpin disulfide are conserved in elapid sequences but are absent in viperids, which possess a conserved C-terminal cysteine involved in an alternative disulfide bridge (residues 49 and 122). (b) Superposition of L. muta PLA2 (green) and that from an elapid species, N. atra (salmon; PDB entry 1poa), highlighting the β-hairpin and α1-helix regions. In L. muta, as in other viperid-derived PLA2s, the absence of the disulfide bridge connecting these elements is compensated by an electrostatic interaction between Lys11 and Glu68.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 82| Part 5| May 2026| Pages 150-159
https://doi.org/10.1107/S2053230X26002736
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