1god

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

spinqualitylabelsall models 1god, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1god is a 1 chain structure with sequence from Cerrophidion godmani. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Phospholipase A(2), with EC number 3.1.1.4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PA22_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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase A2

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