Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system

Mol Cell. 2000 Dec;6(6):1461-72. doi: 10.1016/s1097-2765(00)00142-8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / chemistry
  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Antigens, Bacterial*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Helicobacter pylori / enzymology*
  • Helicobacter pylori / metabolism
  • Helicobacter pylori / pathogenicity
  • Hydrogen Bonding
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protein Subunits
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Virulence Factors*

Substances

  • Antigens, Bacterial
  • Bacterial Proteins
  • Membrane Proteins
  • Protein Subunits
  • Recombinant Proteins
  • Virulence Factors
  • cagA protein, Helicobacter pylori
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Adenosine Triphosphatases

Associated data

  • PDB/1G6O