Preliminary X-ray crystallographic studies of BthTX-II, a myotoxic Asp49-phospholipase A2 with low catalytic activity from Bothrops jararacussu venom.
For the first time, a complete X-ray diffraction data set has been collected from a myotoxic Asp49-phospholipase A2 (Asp49-PLA2) with low catalytic activity (BthTX-II from Bothrops jararacussu venom) and a molecular-replacement solution has been obtained with a dimer in the asymmetric unit. The quaternary structure of BthTX-II resembles the myotoxin Asp49-PLA2 PrTX-III (piratoxin III from B. pirajai venom) and all non-catalytic and myotoxic dimeric Lys49-PLA2s. In contrast, the oligomeric structure of BthTX-II is different from the highly catalytic and non-myotoxic BthA-I (acidic PLA2 from B. jararacussu). Thus, comparison between these structures should add insight into the catalytic and myotoxic activities of bothropic PLA2s.
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Departamento de Física e Biofísica, Instituto de Biociências, UNESP, CP 510, CEP 18618-000, Botucatu-SP, Brazil.
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D000818:Animals; D001216:Asparagine; D017837:Bothrops; D002384:Catalysis; D003435:Crotalid Venoms / Q000737:chemistry / Q000378:metabolism / Q000633:toxicity*; D018360:Crystallography, X-Ray; D007700:Kinetics; D010741:Phospholipases A / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism / Q000633:toxicity*; D054467:Phospholipases A2; D011487:Protein Conformation
D003435:Crotalid Venoms; D001216:Asparagine; D010741:Phospholipases A; D054467:Phospholipases A2