6UZH

Cryo-EM structure of mechanosensitive channel MscS reconstituted into peptidiscs

Summary for 6UZH

• Entry DOI: 10.2210/pdb6uzh/pdb
• EMDB information: 20950 20959 20962
• Descriptor: Small-conductance mechanosensitive channel (1 entity in total)
• Functional Keywords: membrane protein, mechanosensitive channels, mscs, membrane mimetic, peptidisc, transport protein
• Biological source: Escherichia coli
• Total number of polymer chains: 7
• Total formula weight: 231659.81

Authors

Angiulli, G.,Walz, T.,Dhupar, H.S.,Suzuki, H.,Wason, I.S.,Duong Van Hoa, F. (deposition date: 2019-11-15, release date: 2020-03-04, Last modification date: 2025-05-21)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.3 Å)