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1OQS

Crystal Structure of RV4/RV7 Complex

Summary for 1OQS
Entry DOI10.2210/pdb1oqs/pdb
DescriptorPhospholipase A2 RV-7, Phospholipase A2 RV-4 (3 entities in total)
Functional Keywordshydrolase
Biological sourceDaboia russellii siamensis
More
Cellular locationSecreted: P31100 Q02471
Total number of polymer chains8
Total formula weight110079.46
Authors
Perbandt, M.,Betzel, C. (deposition date: 2003-03-11, release date: 2003-09-30, Last modification date: 2024-11-20)
Primary citationPerbandt, M.,Tsai, I.H.,Fuchs, A.,Banumathi, S.,Rajashankar, K.R.,Georgieva, D.,Kalkura, N.,Singh, T.P.,Genov, N.,Betzel, C.
Structure of the heterodimeric neurotoxic complex viperotoxin F (RV-4/RV-7) from the venom of Vipera russelli formosensis at 1.9 A resolution.
Acta Crystallogr.,Sect.D, 59:1679-1687, 2003
Cited by
PubMed Abstract: The presynaptic viperotoxin F is the major lethal component of the venom of Vipera russelli formosensis (Taiwan viper). It is a heterodimer of two highly homologous (65% identity) but oppositely charged subunits: a basic and neurotoxic PLA(2) (RV-4) and an acidic non-toxic component with a very low enzymatic activity (RV-7). The crystal structure of the complex has been determined by molecular replacement and refined to 1.9 A resolution and an R factor of 22.3% with four RV-4/RV-7 complexes in the asymmetric unit, which do not exhibit any local point-group symmetry. The complex formation decreases the accessible surface area of the two subunits by approximately 1425 A(2). Both PLA(2)s are predicted to have very low, if any, anticoagulant activity. The structure of viperotoxin F is compared with that of the heterodimeric neurotoxin vipoxin from the venom of another viper, V. ammodytes meridionalis. The structural basis for the differences between the pharmacological activities of the two toxins is discussed. The neutralization of the negative charge of the major ligand for Ca(2+), Asp49, by intersubunit salt bridges is probably a common mechanism of self-stabilization of heterodimeric Viperinae snake-venom neurotoxins in the absence of bound calcium.
PubMed: 14501106
DOI: 10.1107/S0907444903014987
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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