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4B4A

Structure of the TatC core of the twin arginine protein translocation system

4B4A の概要
エントリーDOI10.2210/pdb4b4a/pdb
分子名称SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, Lauryl Maltose Neopentyl Glycol (2 entities in total)
機能のキーワードtransport protein, tat secretion system, protein translocation
由来する生物種AQUIFEX AEOLICUS
細胞内の位置Cell inner membrane; Multi-pass membrane protein (By similarity): O67305
タンパク質・核酸の鎖数1
化学式量合計29427.77
構造登録者
主引用文献Rollauer, S.E.,Tarry, M.J.,Graham, J.E.,Jaaskelainen, M.,Jager, F.,Johnson, S.,Krehenbrink, M.,Liu, S.,Lukey, M.J.,Marcoux, J.,Mcdowell, M.A.,Rodriguez, F.,Roversi, P.,Stansfeld, P.J.,Robinson, C.V.,Sansom, M.S.P.,Palmer, T.,Hogbom, M.,Berks, B.C.,Lea, S.M.
Structure of the Tatc Core of the Twin-Arginine Protein Transport System.
Nature, 49:210-, 2012
Cited by
PubMed Abstract: The twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, a task that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism.
PubMed: 23201679
DOI: 10.1038/NATURE11683
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.5 Å)
構造検証レポート
Validation report summary of 4b4a
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2026-02-04に公開中

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