1g6o

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Revision as of 22:48, 24 November 2007

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spinqualitylabelsall models 1g6o, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE HELICOBACTER PYLORI ATPASE, HP0525, IN COMPLEX WITH ADP

Overview

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.

About this Structure

1G6O is a Single protein structure of sequence from Helicobacter pylori with ADP and PEG as ligands. Full crystallographic information is available from OCA.

Reference

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

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