6TYI

ExbB-ExbD complex in MSP1E3D1 nanodisc

6TYI の概要

• エントリーDOI: 10.2210/pdb6tyi/pdb
• EMDBエントリー: 20583
• 分子名称: Biopolymer transport protein ExbB, Biopolymer transport protein ExbD, (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE, ... (4 entities in total)
• 機能のキーワード: molecular motor, ton system, membrane protein, transport protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 170796.02

構造登録者

Celia, H.,Botos, I.,Jiang, J.,Buchanan, S.K. (登録日: 2019-08-09, 公開日: 2019-10-16, 最終更新日: 2024-03-20)

主引用文献

Celia, H.,Botos, I.,Ni, X.,Fox, T.,De Val, N.,Lloubes, R.,Jiang, J.,Buchanan, S.K.
Cryo-EM structure of the bacterial Ton motor subcomplex ExbB-ExbD provides information on structure and stoichiometry.
Commun Biol, 2:358-358, 2019

PubMed Abstract: The TonB-ExbB-ExbD molecular motor harnesses the proton motive force across the bacterial inner membrane to couple energy to transporters at the outer membrane, facilitating uptake of essential nutrients such as iron and cobalamine. TonB physically interacts with the nutrient-loaded transporter to exert a force that opens an import pathway across the outer membrane. Until recently, no high-resolution structural information was available for this unique molecular motor. We published the first crystal structure of ExbB-ExbD in 2016 and showed that five copies of ExbB are arranged as a pentamer around a single copy of ExbD. However, our spectroscopic experiments clearly indicated that two copies of ExbD are present in the complex. To resolve this ambiguity, we used single-particle cryo-electron microscopy to show that the ExbB pentamer encloses a dimer of ExbD in its transmembrane pore, and not a monomer as previously reported. The revised stoichiometry has implications for motor function.

PubMed: 31602407
DOI: 10.1038/s42003-019-0604-2

実験手法

ELECTRON MICROSCOPY (3.3 Å)