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Structure-function analysis of PorX Fj , the PorX homolog from Flavobacterium johnsioniae, suggests a role of the CheY-like domain in type IX secretion motor activity.
- Source :
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Scientific reports [Sci Rep] 2024 Mar 19; Vol. 14 (1), pp. 6577. Date of Electronic Publication: 2024 Mar 19. - Publication Year :
- 2024
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Abstract
- The type IX secretion system (T9SS) is a large multi-protein transenvelope complex distributed into the Bacteroidetes phylum and responsible for the secretion of proteins involved in pathogenesis, carbohydrate utilization or gliding motility. In Porphyromonas gingivalis, the two-component system PorY sensor and response regulator PorX participate to T9SS gene regulation. Here, we present the crystal structure of PorX <subscript>Fj</subscript> , the Flavobacterium johnsoniae PorX homolog. As for PorX, the PorX <subscript>Fj</subscript> structure is comprised of a CheY-like N-terminal domain and an alkaline phosphatase-like C-terminal domain separated by a three-helix bundle central domain. While not activated and monomeric in solution, PorX <subscript>Fj</subscript> crystallized as a dimer identical to active PorX. The CheY-like domain of PorX <subscript>Fj</subscript> is in an active-like conformation, and PorX <subscript>Fj</subscript> possesses phosphodiesterase activity, in agreement with the observation that the active site of its phosphatase-like domain is highly conserved with PorX.<br /> (© 2024. The Author(s).)
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 14
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 38503809
- Full Text :
- https://doi.org/10.1038/s41598-024-57089-9