2L16

Solution structure of Bacillus subtilits TatAd protein in DPC micelles

2L16 の概要

• エントリーDOI: 10.2210/pdb2l16/pdb
• 分子名称: Sec-independent protein translocase protein tatAd (1 entity in total)
• 機能のキーワード: membrane protein, protein transport
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Membrane; Single-pass membrane protein: O31467
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8510.84

構造登録者

Hu, Y.,Jin, C. (登録日: 2010-07-23, 公開日: 2010-09-08, 最終更新日: 2024-05-01)

主引用文献

Hu, Y.,Zhao, E.,Li, H.,Xia, B.,Jin, C.
Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis
J.Am.Chem.Soc., 132:15942-15944, 2010

PubMed Abstract: The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive bacteria consists of two essential components, the TatA and TatC proteins. TatA is considered to be a bifunctional subunit, which can form a protein-conducting channel by self-oligomerization and can also participate in substrate recognition. However, the molecular mechanism underlying protein translocation remains elusive. Herein, we report the solution structure of the TatA(d) protein from Bacillus subtilis by NMR spectroscopy, the first structure of the Tat system at atomic resolution. TatA(d) shows an L-shaped structure formed by a transmembrane helix and an amphipathic helix, while the C-terminal tail is largely unstructured. Our results strongly support the postulated topology of TatA(d) in which the transmembrane helix is inserted into the lipid bilayer while the amphipathic helix lies at the membrane-water interface. Moreover, the structure of TatA(d) revealed the structural importance of several conserved residues at the hinge region, thus shedding new light on further elucidation of the protein transport mechanism of the Tat system.

PubMed: 20726548
DOI: 10.1021/ja1053785

実験手法

SOLUTION NMR