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- W2083498141 abstract "The type IV secretion system of Helicobacter pylori consists of 10--15 proteins responsible for transport of the transforming protein CagA into target epithelial cells. Secretion of CagA crucially depends on the hexameric ATPase, HP0525, a member of the VirB11-PulE family. We present the crystal structure of a binary complex of HP0525 bound to ADP. Each monomer consists of two domains formed by the N- and C-terminal halves of the sequence. ADP is bound at the interface between the two domains. In the hexamer, the N- and C-terminal domains form two rings, which together form a chamber open on one side and closed on the other. A model is proposed in which HP0525 functions as an inner membrane pore, the closure and opening of which is regulated by ATP binding and ADP release." @default.
- W2083498141 created "2016-06-24" @default.
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- W2083498141 date "2000-12-01" @default.
- W2083498141 modified "2023-09-30" @default.
- W2083498141 title "Crystal Structure of the Hexameric Traffic ATPase of the Helicobacter pylori Type IV Secretion System" @default.
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- W2083498141 doi "https://doi.org/10.1016/s1097-2765(00)00142-8" @default.
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