6UZ2

Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 1

6UZ2 の概要

• エントリーDOI: 10.2210/pdb6uz2/pdb
• EMDBエントリー: 20950 20959 20962
• 分子名称: Lipid A export ATP-binding/permease protein MsbA (1 entity in total)
• 機能のキーワード: membrane protein, abc transporter, membrane mimetic, peptidisc, translocase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 133666.22

構造登録者

Angiulli, G.,Walz, T.,Dhupar, H.S.,Suzuki, H.,Wason, I.S.,Duong Van Hoa, F. (登録日: 2019-11-14, 公開日: 2020-03-04, 最終更新日: 2025-05-14)

主引用文献

Angiulli, G.,Dhupar, H.S.,Suzuki, H.,Wason, I.S.,Duong Van Hoa, F.,Walz, T.
New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins.
Elife, 9:-, 2020

PubMed Abstract: Previously we introduced peptidiscs as an alternative to detergents to stabilize membrane proteins in solution (Carlson et al., 2018). Here, we present 'on-gradient' reconstitution, a new gentle approach for the reconstitution of labile membrane-protein complexes, and used it to reconstitute reaction center complexes, demonstrating that peptidiscs can adapt to transmembrane domains of very different sizes and shapes. Using the conventional 'on-bead' approach, we reconstituted proteins MsbA and MscS and find that peptidiscs stabilize them in their native conformation and allow for high-resolution structure determination by cryo-electron microscopy. The structures reveal that peptidisc peptides can arrange around transmembrane proteins differently, thus revealing the structural basis for why peptidiscs can stabilize such a large variety of membrane proteins. Together, our results establish the gentle and easy-to-use peptidiscs as a potentially universal alternative to detergents as a means to stabilize membrane proteins in solution for structural and functional studies.

PubMed: 32125274
DOI: 10.7554/eLife.53530

実験手法

ELECTRON MICROSCOPY (4.2 Å)