Crystal structure of a snake venom cardiotoxin.
Cardiotoxin VII4 from Naja mossambica mossambica crystallizes in space group P61 (a = b = 73.9 A; c = 59.0 A) with two molecules of toxin (molecular mass = 6715 Da) in the asymmetric unit. The structure was solved by using a combination of multiple isomorphous replacement and density modification methods. Model building and least-squares refinement led to an agreement factor of 27% for a data set to 3-A resolution prior to any inclusion of solvent molecules. The topology of the molecule is similar to that found in short and long snake neurotoxins, which block the nicotinic acetylcholine receptor. Major differences occur in the conformation of the central loop, resulting in a change in the concavity of the molecule. Hydrophobic residues are clustered in two distinct areas. The existence of stable dimeric entities in the crystalline state, with the formation of a six-stranded antiparallel beta sheet, may be functionally relevant.
Rees
B
B
Samama
J P
JP
Thierry
J C
JC
Gilibert
M
M
Fischer
J
J
Schweitz
H
H
Lazdunski
M
M
Moras
D
D
D000595:Amino Acid Sequence; D004179:Cobra Cardiotoxin Proteins / Q000302:isolation & purification; D004546:Elapid Venoms / Q000302:isolation & purification; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction
D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms