4HTT

Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM

4HTT の概要

• エントリーDOI: 10.2210/pdb4htt/pdb
• 関連するPDBエントリー: 4HTS
• 分子名称: Sec-independent protein translocase protein TatC, Lysozyme (1 entity in total)
• 機能のキーワード: twin arginine translocase receptor, membrane, hydrolase
• 由来する生物種: Aquifex aeolicus VF5; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94689.98

構造登録者

Ramasamy, S.,Suloway, C.J.M.,Clemons Jr., W.M. (登録日: 2012-11-01, 公開日: 2013-05-01, 最終更新日: 2024-02-28)

主引用文献

Ramasamy, S.,Abrol, R.,Suloway, C.J.,Clemons, W.M.
The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation.
Structure, 21:777-788, 2013

PubMed Abstract: In bacteria, two signal-sequence-dependent secretion pathways translocate proteins across the cytoplasmic membrane. Although the mechanism of the ubiquitous general secretory pathway is becoming well understood, that of the twin-arginine translocation pathway, responsible for translocation of folded proteins across the bilayer, is more mysterious. TatC, the largest and most conserved of three integral membrane components, provides the initial binding site of the signal sequence prior to pore assembly. Here, we present two crystal structures of TatC from the thermophilic bacteria Aquifex aeolicus at 4.0 Å and 6.8 Å resolution. The membrane architecture of TatC includes a glove-shaped structure with a lipid-exposed pocket predicted by molecular dynamics to distort the membrane. Correlating the biochemical literature to these results suggests that the signal sequence binds in this pocket, leading to structural changes that facilitate higher order assemblies.

PubMed: 23583035
DOI: 10.1016/j.str.2013.03.004

実験手法

X-RAY DIFFRACTION (6.8 Å)