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腺嘌呤与大肠杆菌O157:H7的蛋白质毒素Stx2的结合。

Binding of adenine to Stx2, the protein toxin from Escherichia coli O157:H7.

作者信息

Fraser Marie E, Cherney Maia M, Marcato Paola, Mulvey George L, Armstrong Glen D, James Michael N G

机构信息

Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary AB T2N 1N4, Canada.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt 7):627-30. doi: 10.1107/S1744309106021968. Epub 2006 Jun 26.

Abstract

Stx2 is a protein toxin whose catalytic subunit acts as an N-glycosidase to depurinate a specific adenine base from 28S rRNA. In the holotoxin, the catalytic portion, A1, is linked to the rest of the A subunit, A2, and A2 interacts with the pentameric ring formed by the five B subunits. In order to test whether the holotoxin is active as an N-glycosidase, Stx2 was crystallized in the presence of adenosine and adenine. The crystals diffracted to approximately 1.8 angstroms and showed clear electron density for adenine in the active site. Adenosine had been cleaved, proving that Stx2 is an active N-glycosidase. While the holotoxin is active against small substrates, it would be expected that the B subunits would interfere with the binding of the 28S rRNA.

摘要

志贺毒素2(Stx2)是一种蛋白质毒素,其催化亚基作为N-糖苷酶,从28S核糖体RNA上去除特定的腺嘌呤碱基。在全毒素中,催化部分A1与A亚基的其余部分A2相连,并且A2与由五个B亚基形成的五聚体环相互作用。为了测试全毒素作为N-糖苷酶是否具有活性,在腺苷和腺嘌呤存在的情况下使Stx2结晶。晶体衍射至约1.8埃,并在活性位点显示出腺嘌呤的清晰电子密度。腺苷已被切割,证明Stx2是一种活性N-糖苷酶。虽然全毒素对小分子底物具有活性,但可以预期B亚基会干扰28S核糖体RNA的结合。

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