1G6O

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

Summary for 1G6O

• Entry DOI: 10.2210/pdb1g6o/pdb
• Descriptor: CAG-ALPHA, ADENOSINE-5'-DIPHOSPHATE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: atpase, type iv secretion system, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 2
• Total formula weight: 77213.49

Authors

Yeo, H.J.,Savvides, S.N.,Herr, A.B.,Lanka, E.,Waksman, G.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2000-11-07, release date: 2001-01-24, Last modification date: 2024-11-20)

Primary citation

Yeo, H.J.,Savvides, S.N.,Herr, A.B.,Lanka, E.,Waksman, G.
Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system.
Mol.Cell, 6:1461-1472, 2000

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.

PubMed: 11163218
DOI: 10.1016/S1097-2765(00)00142-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)