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6H8F

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

6H8F の概要
エントリーDOI10.2210/pdb6h8f/pdb
関連するPDBエントリー6H8E 6HS5 6HS6
分子名称TssA (2 entities in total)
機能のキーワードalpha-helical protein, type vi secretion system component, tssa, transport protein
由来する生物種Burkholderia cenocepacia H111
タンパク質・核酸の鎖数2
化学式量合計17185.34
構造登録者
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.78 Å)
構造検証レポート
Validation report summary of 6h8f
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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