6IZ8

Crystal Structure of TagF from Pseudomonas aeruginosa

Summary for 6IZ8

• Entry DOI: 10.2210/pdb6iz8/pdb
• Descriptor: Type VI secretion-associated protein (2 entities in total)
• Functional Keywords: type vi secretion system, tagf, longin domain, denn family, signaling protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 5
• Total formula weight: 130873.11

Authors

Chang, J.H.,Ok, C.K. (deposition date: 2018-12-18, release date: 2019-12-18, Last modification date: 2024-03-27)

Primary citation

Ok, C.K.,Chang, J.H.
Crystal Structure of the Type VI Secretion System Accessory Protein TagF from Pseudomonas Aeruginosa.
Protein Pept.Lett., 26:204-214, 2019

PubMed Abstract: Type VI Secretion System (T6SS) has been found in approximately onequarter of the gram-negative bacterial species, and its structural characteristics appear to slightly differ from species to species. The genes encoding T6SS are designated as type six secretion A-M (tssA-M). The expression of the tss gene cluster is regulated by various accessory genes, designated as type VI-associated genes A-P (tagA-P). Tag family proteins have been commonly found in bacteria expressing T6SS but not in all bacterial species. For instance, the tag gene cluster is well-conserved in Pseudomonas aeruginosa (Pa). The PaTagF protein has large homology with ImpM in Rhizobium leguminosarum and SciT in Salmonella enterica. The overexpression of PaTagF represses T6SS complex accumulation and suppresses T6SS antibacterial activity. Thus, the functions of TagF are mediated through direct interactions with the forkhead-associated protein Fha, as evident from the results of the yeast-two hybrid assays. Fha is involved in recruiting a membrane-associated complex either in threonine phosphorylation pathway-dependent or - independent manner. However, functional reports of the tag gene cluster are still limited.

PubMed: 30659530
DOI: 10.2174/0929866526666190119121859

Experimental method

X-RAY DIFFRACTION (2.7 Å)