1g6o

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

spinqualitylabelsall models 1g6o, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1g6o is a 2 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: ADP, MSE, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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