EMDB/PDB/SASBDBから引用されている文献のデータベース

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構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
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IF	>30 >20 >10 >5 all

タイトル	Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 106, Issue 32, Page 13284-13289, Year 2009
掲載日	2009年8月11日
著者	Michael J Tarry / Eva Schäfer / Shuyun Chen / Grant Buchanan / Nicholas P Greene / Susan M Lea / Tracy Palmer / Helen R Saibil / Ben C Berks /
PubMed 要旨	The Tat system transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. In Escherichia coli substrate proteins initially bind to the ...The Tat system transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. In Escherichia coli substrate proteins initially bind to the integral membrane TatBC complex which then recruits the protein TatA to effect translocation. Overproduction of TatBC and the substrate protein SufI in the absence of TatA led to the accumulation of TatBC-SufI complexes that could be purified using an affinity tag on the substrate. Three-dimensional structures of the TatBC-SufI complexes and unliganded TatBC were obtained by single-particle electron microscopy and random conical tilt reconstruction. Comparison of the structures shows that substrate molecules bind on the periphery of the TatBC complex and that substrate binding causes a significant reduction in diameter of the TatBC part of the complex. Although the TatBC complex contains multiple copies of the signal peptide-binding TatC protomer, purified TatBC-SufI complexes contain only 1 or 2 SufI molecules. Where 2 substrates are present in the TatBC-SufI complex, they are bound at adjacent sites. These observations imply that only certain TatC protomers within the complex interact with substrate or that there is a negative cooperativity of substrate binding. Similar TatBC-substrate complexes can be generated by an alternative in vitro reconstitution method and using a different substrate protein.
リンク	Proc Natl Acad Sci U S A / PubMed:19666509 / PubMed Central
手法	EM (単粒子)
構造データ	EMDB-1632: Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. 手法: EM (単粒子) EMDB-1633: Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. 手法: EM (単粒子) EMDB-1634: Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. 手法: EM (単粒子) EMDB-1635: Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. 手法: EM (単粒子)
由来	Escherichia coli (大腸菌)