6HS6

C-terminal domain of the TssA component of the type VI secretion system from Burkholderia cenocepacia

Summary for 6HS6

• Entry DOI: 10.2210/pdb6hs6/pdb
• Related: 6H8E 6H8F 6HS5
• Descriptor: Type VI secretion protein ImpA (1 entity in total)
• Functional Keywords: alpha-helical protein, type vi secretion system component, tssa, transport protein
• Biological source: Burkholderia cenocepacia H111
• Total number of polymer chains: 8
• Total formula weight: 68741.38

Authors

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. (deposition date: 2018-09-28, release date: 2018-11-21, Last modification date: 2024-05-15)

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 (3.08 Å)