2YHS

Structure of the E. coli SRP receptor FtsY

2YHS の概要

• エントリーDOI: 10.2210/pdb2yhs/pdb
• 関連するPDBエントリー: 1FTS 2XXA
• 分子名称: CELL DIVISION PROTEIN FTSY, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: cell cycle, protein targeting, simibi class gtpase, gtp-binding, membrane, nucleotide-binding, signal recognition particle, protein transport
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein: P10121
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55708.22

構造登録者

Stjepanovic, G.,Bange, G.,Wild, K.,Sinning, I. (登録日: 2011-05-05, 公開日: 2011-05-18, 最終更新日: 2023-12-20)

主引用文献

Stjepanovic, G.,Kapp, K.,Bange, G.,Graf, C.,Parlitz, R.,Wild, K.,Mayer, M.P.,Sinning, I.
Lipids Trigger a Conformational Switch that Regulates Signal Recognition Particle (Srp)-Mediated Protein Targeting.
J.Biol.Chem., 286:23489-, 2011

PubMed Abstract: Co-translational protein targeting to the membrane is mediated by the signal recognition particle and its receptor (FtsY). Their homologous GTPase domains interact at the membrane and form a heterodimer in which both GTPases are activated. The prerequisite for protein targeting is the interaction of FtsY with phospholipids. However, the mechanism of FtsY regulation by phospholipids remained unclear. Here we show that the N terminus of FtsY (A domain) is natively unfolded in solution and define the complete membrane-targeting sequence. We show that the membrane-targeting sequence is highly dynamic in solution, independent of nucleotides and directly responds to the density of anionic phospholipids by a random coil-helix transition. This conformational switch is essential for tethering FtsY to membranes and activates the GTPase for its subsequent interaction with the signal recognition particle. Our results underline the dynamics of lipid-protein interactions and their importance in the regulation of protein targeting and translocation across biological membranes.

PubMed: 21543314
DOI: 10.1074/JBC.M110.212340

実験手法

X-RAY DIFFRACTION (1.6 Å)