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Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase

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Date
2007-11
ICR Author
Bayliss, Richard
Author
Hare, S
Fischer, W
Williams, R
Terradot, L
Bayliss, R
Haas, R
Waksman, G
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Type
Journal Article
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Abstract
Helicobacter 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.
URI
https://repository.icr.ac.uk/handle/internal/2463
DOI
https://doi.org/10.1038/sj.emboj.7601904
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  • Other ICR Research
Language
eng
License start date
2007-11
Citation
EMBO JOURNAL, 2007, 26 pp. 4926 - 4934
Publisher
WILEY-BLACKWELL

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