6Y86

Active YidC insertase crystal structure with the first transmembrane domain resolved

6Y86 の概要

• エントリーDOI: 10.2210/pdb6y86/pdb
• 分子名称: Membrane protein insertase YidC (1 entity in total)
• 機能のキーワード: insertase and chaperone, membrane protein
• 由来する生物種: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49201.25

構造登録者

Li, X.D.,Nass, K. (登録日: 2020-03-03, 公開日: 2021-09-22, 最終更新日: 2026-03-04)

主引用文献

Nass, K.J.,Ilie, I.M.,Saller, M.J.,Driessen, A.J.M.,Caflisch, A.,Kammerer, R.A.,Li, X.
The role of the N-terminal amphipathic helix in bacterial YidC: Insights from functional studies, the crystal structure and molecular dynamics simulations.
Biochim Biophys Acta Biomembr, 1864:183825-183825, 2022

PubMed Abstract: The evolutionary conserved YidC is a unique dual-function membrane protein that adopts insertase and chaperone conformations. The N-terminal helix of Escherichia coli YidC functions as an uncleaved signal sequence and is important for membrane insertion and interaction with the Sec translocon. Here, we report the first crystal structure of Thermotoga maritima YidC (TmYidC) including the N-terminal amphipathic helix (N-AH) (PDB ID: 6Y86). Molecular dynamics simulations show that N-AH lies on the periplasmic side of the membrane bilayer forming an angle of about 15° with the membrane surface. Our functional studies suggest a role of N-AH for the species-specific interaction with the Sec translocon. The reconstitution data and the superimposition of TmYidC with known YidC structures suggest an active insertase conformation for YidC. Molecular dynamics (MD) simulations of TmYidC provide evidence that N-AH acts as a membrane recognition helix for the YidC insertase and highlight the flexibility of the C1 region underlining its ability to switch between insertase and chaperone conformations. A structure-based model is proposed to rationalize how YidC performs the insertase and chaperone functions by re-positioning of N-AH and the other structural elements.

PubMed: 34871574
DOI: 10.1016/j.bbamem.2021.183825

実験手法

X-RAY DIFFRACTION (3.4 Å)