2QOG
Crotoxin B, the basic PLA2 from Crotalus durissus terrificus.
Summary for 2QOG
| Entry DOI | 10.2210/pdb2qog/pdb |
| Related | 2OK9 2OQD |
| Descriptor | Phospholipase A2 CB2, Phospholipase A2 CB1, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | crotoxin b cd-cdt basic-pla2, calcium, hydrolase, lipid degradation, metal-binding, secreted, neurotoxin, presynaptic neurotoxin |
| Biological source | Crotalus durissus terrificus (tropical rattlesnake) More |
| Cellular location | Secreted: P24027 P62022 |
| Total number of polymer chains | 4 |
| Total formula weight | 57083.85 |
| Authors | Marchi-Salvador, D.P.,Correa, L.C.,Fontes, M.R.M. (deposition date: 2007-07-20, release date: 2008-04-01, Last modification date: 2024-11-20) |
| Primary citation | Marchi-Salvador, D.P.,Correa, L.C.,Magro, A.J.,Oliveira, C.Z.,Soares, A.M.,Fontes, M.R. Insights into the role of oligomeric state on the biological activities of crotoxin: crystal structure of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom. Proteins, 72:883-891, 2008 Cited by PubMed Abstract: Crotoxin B (CB or Cdt PLA(2)) is a basic Asp49-PLA(2) found in the venom of Crotalus durissus terrificus and it is one of the subunits that constitute the crotoxin (Cro). This heterodimeric toxin, main component of the C. d. terrificus venom, is completed by an acidic, nontoxic, and nonenzymatic component (crotoxin A, CA or crotapotin), and it is related to important envenomation effects such as neurological disorders, myotoxicity, and renal failure. Although Cro has been crystallized since 1938, no crystal structure of this toxin or its subunits is currently available. In this work, the authors present the crystal structure of a novel tetrameric complex formed by two dimers of crotoxin B isoforms (CB1 and CB2). The results suggest that these assemblies are stable in solution and show that Ser1 and Glu92 of CB1 and CB2, respectively, play an important role in the oligomerization. The tetrameric and dimeric conformations resulting from the association of the isoforms may increase the neurotoxicity of the toxin CB by the creation of new binding sites, which could improve the affinity of the molecular complexes to the presynaptic membrane. PubMed: 18275084DOI: 10.1002/prot.21980 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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