Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system.
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Yeo HJ, Savvides SN, Herr AB, Lanka E, Waksman G
Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system.
Mol Cell. 2000 Dec;6(6):1461-72.
- PubMed ID
- 11163218 [ View in PubMed]
- 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.