Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani.
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.
Arni
R K
RK
Department of Physics, IBILCE/UNESP, São José do Rio Preto-SP, Brazil. arni@df.ibilce.unesp.br
Fontes
M R
MR
Barberato
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Gutiérrez
J M
JM
Díaz
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Ward
R J
RJ
D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D054501:Group II Phospholipases A2; D008958:Models, Molecular; D009498:Neurotoxins / Q000737:chemistry* / Q000302:isolation & purification; D010741:Phospholipases A / Q000737:chemistry* / Q000302:isolation & purification; D054467:Phospholipases A2; D011108:Polymers / Q000737:chemistry; D017433:Protein Structure, Secondary; D030162:Reptilian Proteins; D012542:Scattering, Radiation; D017386:Sequence Homology, Amino Acid; D014965:X-Rays
D003435:Crotalid Venoms; D009498:Neurotoxins; D011108:Polymers; D030162:Reptilian Proteins; D010741:Phospholipases A; D054501:Group II Phospholipases A2; D054467:Phospholipases A2; C113262:myotoxin II, Bothrops godmani