1GOD

MONOMERIC LYS-49 PHOSPHOLIPASE A2 HOMOLOGUE ISOLATED FROM THE VENOM OF CERROPHIDION (BOTHROPS) GODMANI

Summary for 1GOD

• Entry DOI: 10.2210/pdb1god/pdb
• Descriptor: PROTEIN (PHOSPHOLIPASE A2) (2 entities in total)
• Functional Keywords: lys49-phospholipase a2, snake venom, bothrops, hydrolase
• Biological source: Cerrophidion godmani
• Cellular location: Secreted: P81165
• Total number of polymer chains: 1
• Total formula weight: 13733.95

Authors

Arni, R.K.,Fontes, M.R.M.,Barberato, C.,Gutierrez, J.M.,Diaz-Oreiro, C.,Ward, R.J. (deposition date: 1999-04-16, release date: 1999-04-23, Last modification date: 2024-10-09)

Primary citation

Arni, R.K.,Fontes, M.R.,Barberato, C.,Gutierrez, J.M.,Diaz, C.,Ward, R.J.
Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani.
Arch.Biochem.Biophys., 366:177-182, 1999

PubMed Abstract: 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.

PubMed: 10356281
DOI: 10.1006/abbi.1999.1210

Experimental method

X-RAY DIFFRACTION (2.8 Å)