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
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Diphosphate / chemistry
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Adenosine Diphosphate / metabolism
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / metabolism
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Antigens, Bacterial*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Binding Sites
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Crystallography, X-Ray
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Helicobacter pylori / enzymology*
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Helicobacter pylori / metabolism
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Helicobacter pylori / pathogenicity
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Hydrogen Bonding
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Models, Biological
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Models, Molecular
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Molecular Sequence Data
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Protein Binding
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Protein Structure, Quaternary
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Protein Structure, Tertiary
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Protein Subunits
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Alignment
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Virulence Factors*
Substances
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Antigens, Bacterial
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Bacterial Proteins
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Membrane Proteins
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Protein Subunits
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Recombinant Proteins
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Virulence Factors
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cagA protein, Helicobacter pylori
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Adenosine Diphosphate
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Adenosine Triphosphate
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Adenosine Triphosphatases