6G7C

Nt2-CTD domains of the TssA component from the type VI secretion system of Aeromonas hydrophila.

Summary for 6G7C

• Entry DOI: 10.2210/pdb6g7c/pdb
• Descriptor: ImpA-related domain protein (1 entity in total)
• Functional Keywords: type vi secretion system component, alpha helical protein, tssa, aeromonas hydrophila, transport protein
• Biological source: Aeromonas hydrophila subsp. hydrophila ATCC 7966
• Total number of polymer chains: 10
• Total formula weight: 295903.73

Authors

Dix, S.D.,Owen, H.J.,Sun, R.,Ahmad, A.,Shastri, S.,Spiewak, H.L.,Mosby, D.J.,Harris, M.J.,Batters, S.L.,Tzokov, S.B.,Sedelnikova, S.E.,Baker, P.J.,Bullough, P.A.,Rice, D.W.,Thomas, M.S. (deposition date: 2018-04-05, release date: 2018-11-21, Last modification date: 2024-05-08)

Primary citation

Dix, S.R.,Owen, H.J.,Sun, R.,Ahmad, A.,Shastri, S.,Spiewak, H.L.,Mosby, D.J.,Harris, M.J.,Batters, S.L.,Brooker, T.A.,Tzokov, S.B.,Sedelnikova, S.E.,Baker, P.J.,Bullough, P.A.,Rice, D.W.,Thomas, M.S.
Structural insights into the function of type VI secretion system TssA subunits.
Nat Commun, 9:4765-4765, 2018

PubMed Abstract: The type VI secretion system (T6SS) is a multi-protein complex that injects bacterial effector proteins into target cells. It is composed of a cell membrane complex anchored to a contractile bacteriophage tail-like apparatus consisting of a sharpened tube that is ejected by the contraction of a sheath against a baseplate. We present structural and biochemical studies on TssA subunits from two different T6SSs that reveal radically different quaternary structures in comparison to the dodecameric E. coli TssA that arise from differences in their C-terminal sequences. Despite this, the different TssAs retain equivalent interactions with other components of the complex and position their highly conserved N-terminal ImpA_N domain at the same radius from the centre of the sheath as a result of their distinct domain architectures, which includes additional spacer domains and highly mobile interdomain linkers. Together, these variations allow these distinct TssAs to perform a similar function in the complex.

PubMed: 30420757
DOI: 10.1038/s41467-018-07247-1

Experimental method

X-RAY DIFFRACTION (3.13 Å)