8P6F

Crystal structure of PorX-Fj

Summary for 8P6F

• Entry DOI: 10.2210/pdb8p6f/pdb
• Descriptor: Response regulator receiver domain-containing protein, MAGNESIUM ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: type ix secretion system, flavobacterium johnsoniae, two-component system, response regulator, unknown function
• Biological source: Flavobacterium johnsoniae
• Total number of polymer chains: 2
• Total formula weight: 126376.05

Authors

Leone, P. (deposition date: 2023-05-26, release date: 2024-04-03)

Primary citation

Zammit, M.,Bartoli, J.,Kellenberger, C.,Melani, P.,Roussel, A.,Cascales, E.,Leone, P.
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.
Sci Rep, 14:6577-6577, 2024

PubMed 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, the Flavobacterium johnsoniae PorX homolog. As for PorX, the PorX 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 crystallized as a dimer identical to active PorX. The CheY-like domain of PorX is in an active-like conformation, and PorX possesses phosphodiesterase activity, in agreement with the observation that the active site of its phosphatase-like domain is highly conserved with PorX.

PubMed: 38503809
DOI: 10.1038/s41598-024-57089-9

Experimental method

X-RAY DIFFRACTION (2 Å)