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Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase
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posted on 2023-06-09, 08:02 authored by Stephen Hare, Wolfgang Fischer, Robert Williams, Laurent Terradot, Richard Bayliss, Rainer Haas, Gabriel WaksmanHelicobacter pylori is one of the world's most successful human pathogens causing gastric ulcers and cancers. A key virulence factor of H. pylori is the Cag pathogenicity island, which encodes a type IV secretion system. HP0525 is an essential component of the Cag system and acts as an inner membrane associated ATPase. HP0525 forms double hexameric ring structures, with the C-terminal domains (CTDs) forming a closed ring and the N-terminal domains (NTDs) forming a dynamic, open ring. Here, the crystal structure of HP0525 in complex with a fragment of HP1451, a protein of previously unknown function, is reported. The HP1451 construct consists of two domains similar to nucleic acid-binding domains. Two HP1451 molecules bind to the HP0525 NTDs on opposite sides of the hexamer, locking it in the closed form and forming a partial lid over the HP0525 chamber. From the structure, it is suggested that HP1451 acts as an inhibitory factor of HP0525 to regulate Cag-mediated secretion, a suggestion confirmed by results of in vitro ATPase assay and in vivo pull-down experiments.
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Publication status
- Published
Journal
EMBO JournalISSN
0261-4189Publisher
EMBO PressExternal DOI
Issue
23Volume
26Page range
4926-4934Department affiliated with
- Biochemistry Publications
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- No
Peer reviewed?
- Yes
Legacy Posted Date
2017-09-21Usage metrics
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