Preliminary cryocrystallography analysis of an eumenine mastoparan toxin isolated from the venom of the wasp Anterhynchium flavomarginatum micado.
Mastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, such as mast cell degranulation, hemolytic activity and also reveals antimicrobial activity. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized. At room temperature these crystals diffracted to 2.8 A resolution. However, upon cooling to cryogenic temperature around 85 K, the original resolution limit could be improved to 2.0 A. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation.
Delatorre
P
P
Departamento de Física--IBILCE, UNESP, São José Rio Preto, SP, Brazil.
Olivieri
J R
JR
Ruggiero Neto
J
J
Lorenzi
C C
CC
Canduri
F
F
Fadel
V
V
Konno
K
K
Palma
M S
MS
Yamane
T
T
de Azevedo
W F
WF
D000818:Animals; D003080:Cold Temperature; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D019476:Insect Proteins / Q000737:chemistry* / Q000302:isolation & purification; D014862:Wasp Venoms / Q000737:chemistry* / Q000302:isolation & purification; D014863:Wasps / Q000378:metabolism*
D019476:Insect Proteins; D014862:Wasp Venoms; C412288:eumenine mastoparan-AF