9MLE
Crystal structure of Asp49 Phospholipase A2 isolated from Lachesis muta
Summary for 9MLE
| Entry DOI | 10.2210/pdb9mle/pdb |
| Descriptor | Phospholipase A2, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | phospholipase a2, lachesis muta, toxin, venom, hydrolase |
| Biological source | Lachesis muta |
| Total number of polymer chains | 2 |
| Total formula weight | 28234.85 |
| Authors | Leonardo, D.A.,Vargas, J.A.,Pereira, H.M.,Garratt, R.C. (deposition date: 2024-12-19, release date: 2026-05-13) |
| Primary citation | 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 Ramirez, J.L.J.,Leonardo, D.A. Crystal structure and functional characterization of an Asp49 phospholipase A 2 from the bushmaster (Lachesis muta). Acta Crystallogr.,Sect.F, 82:150-159, 2026 Cited by PubMed Abstract: Snake-venom phospholipases A (PLAs) are small, structurally conserved enzymes that contribute significantly to the pathophysiology of envenomation. Here, we report the purification and crystal structure of an Asp49-PLA isolated from the venom of Lachesis muta, a pit viper from the Peruvian Amazon. The enzyme was purified using ion-exchange and size-exclusion chromatography and exhibited phospholipase activity in a dose- and time-dependent egg-yolk degradation assay. Pure protein crystals were obtained in space group P622 and diffracted to 2.36 Å resolution, with two molecules in the asymmetric unit. The structure reveals the canonical fold of catalytically active group II PLAs, with a bound Ca ion and a MES molecule in the active site of one monomer. Seven disulfide bonds stabilize the structure, although one bridge typically associated with the β-hairpin is absent and is replaced by a salt bridge as in other viperid PLAs. PISA analysis suggests a potential tetrameric assembly composed of two AB dimers generating an interface between two A subunits (A-A'). Electrostatic surface mapping reveals a notable positively charged channel at the A-A' interface, like that seen for a basic PLA homodimer from Crotalus durissus terrificus in which the two active sites lie accessible to the membrane. This study presents the first structural and enzymatic analysis of an Asp49-PLA from L. muta and provides insights into its oligomeric assembly, electrostatic landscape and potential adaptations relevant to its role in venom toxicity. PubMed: 41944125DOI: 10.1107/S2053230X26002736 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.36 Å) |
Structure validation
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