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...

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Veröffentlicht in:Journal of structural biology 2007-10, Vol.160 (1), p.28-34
Hauptverfasser: Liu, ShengQuan, Wang, Feng, Tang, Lin, Gui, WenJun, Cao, Peng, Liu, XiaoQin, Poon, Alice Wing-Sem, Shaw, Pang-Chui, Jiang, Tao
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Sprache:eng
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Zusammenfassung: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.
ISSN:1047-8477
DOI:10.1016/j.jsb.2007.06.005