Crystallization and preliminary X-ray diffraction analysis of myotoxin I, a Lys49-phospholipase A2 from Bothrops moojeni.
A new myotoxic Lys49-phospholipase A2 isolated from Bothrops moojeni snake venom has been crystallized. The crystals diffracted to 2.18 A resolution using a synchrotron-radiation source and belong to space group C2. The unit-cell parameters are a = 56.8, b = 125.0, c = 64.7 A, beta = 105.5 degrees. Preliminary analysis indicates the presence of four molecules in the asymmetric unit. This may suggest a new quaternary structure for this Lys49-phospholipase A2 in contrast to the dimeric and monomeric structures solved so far for this class of proteins.
Marchi-Salvador
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Departamento de Física e Biofísica-IB, UNESP, CP 510, CEP 18618-000, Botucatu-SP, Brazil.
Silveira
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LB
Soares
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AM
Fontes
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MR
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004058:Diffusion; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D054501:Group II Phospholipases A2; D007525:Isoelectric Focusing; D008239:Lysine / Q000737:chemistry*; D010741:Phospholipases A / Q000737:chemistry*; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D030162:Reptilian Proteins; D012910:Snake Venoms / Q000378:metabolism*; D012911:Snakes; D017356:Synchrotrons; D014961:X-Ray Diffraction
D030162:Reptilian Proteins; D012910:Snake Venoms; D010741:Phospholipases A; D054501:Group II Phospholipases A2; C076780:myotoxin I; D008239:Lysine