Structural highlights
Function
PA2H2_CERGO Snake venom phospholipase A2 (PLA2) that lacks enzymatic activity and shows myotoxicity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani.,Arni RK, Fontes MR, Barberato C, Gutierrez JM, Diaz C, Ward RJ Arch Biochem Biophys. 1999 Jun 15;366(2):177-82. PMID:10356281[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Arni RK, Fontes MR, Barberato C, Gutierrez JM, Diaz C, Ward RJ. 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. PMID:10356281 doi:10.1006/abbi.1999.1210
