Crystal structure of mastoparan from Polistes jadwagae at 1.2 A resolution.
Mastoparans, a group of amphiphilic tetradecapeptides, are the major peptides in social wasp venoms and possess a variety of biological activities. Here we report the first crystal structure of mastoparan from Polistes jadwagae (MP-PJ) at 1.2 A resolution. The crystals belong to the space group P2(1) with eight molecules in an asymmetric unit. In contrast to the previous observations that the alpha-helical conformation only exists in the membrane-bound state of mastoparans, all of the MP-PJ molecules are in possession of the alpha-helical conformation even in the absence of trifluorethanol or detergents in the crystallization system. The high-resolution structure enables us to compare the conformation differences of MP-PJ with NMR results of other mastoparans. Together with biochemical results, we propose that the interactions between mastoparan molecules play an important role in forming the alpha-helical conformation, which is highly related to their biological activities.
Liu
ShengQuan
S
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.
Wang
Feng
F
Tang
Lin
L
Gui
WenJun
W
Cao
Peng
P
Liu
XiaoQin
X
Poon
Alice Wing-Sem
AW
Shaw
Pang-Chui
PC
Jiang
Tao
T
D000818:Animals; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D020349:Surface Plasmon Resonance
D010455:Peptides; C071124:polistes mastoparan