Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani

Arch Biochem Biophys. 1999 Jun 15;366(2):177-82. doi: 10.1006/abbi.1999.1210.


Lys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we have solved the crystal structure of myotoxin-II, a Lys49-PLA2 isolated from the venom of Cerrophidion (Bothrops) godmani (godMT-II) at 2.8 A resolution by molecular replacement. The final model has been refined to a final crystallografic residual (Rfactor) of 18.8% (Rfree = 28.2%), with excellent stereochemistry. godMT-II is also monomeric in the crystalline state, and small-angle X-ray scattering results demonstrate that the protein is monomeric in solution under fisicochemical conditions similar to those used in the crystallographic studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bothrops
  • Crotalid Venoms / chemistry*
  • Crotalid Venoms / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Group II Phospholipases A2
  • Models, Molecular
  • Neurotoxins / chemistry*
  • Neurotoxins / isolation & purification
  • Phospholipases A / chemistry*
  • Phospholipases A / isolation & purification
  • Phospholipases A2
  • Polymers / chemistry
  • Protein Structure, Secondary
  • Reptilian Proteins
  • Scattering, Radiation
  • Sequence Homology, Amino Acid*
  • X-Rays


  • Crotalid Venoms
  • Neurotoxins
  • Polymers
  • Reptilian Proteins
  • Phospholipases A
  • Group II Phospholipases A2
  • Phospholipases A2
  • myotoxin II, Bothrops godmani

Associated data

  • PDB/1GOD