6PWO

MscS DDM

Summary for 6PWO

• Entry DOI: 10.2210/pdb6pwo/pdb
• EMDB information: 20508 20509 20510
• Descriptor: Small-conductance mechanosensitive channel (1 entity in total)
• Functional Keywords: mscs, ddm, mechanosensitive channel of small conductance, mechanosensitive, channel, membrane protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 7
• Total formula weight: 218436.25

Authors

Reddy, B.G.,Perozo, E. (deposition date: 2019-07-23, release date: 2020-01-08, Last modification date: 2024-03-20)

Primary citation

Reddy, B.,Bavi, N.,Lu, A.,Park, Y.,Perozo, E.
Molecular basis of force-from-lipids gating in the mechanosensitive channel MscS.
Elife, 8:-, 2019

PubMed Abstract: Prokaryotic mechanosensitive (MS) channels open by sensing the physical state of the membrane. As such, lipid-protein interactions represent the defining molecular process underlying mechanotransduction. Here, we describe cryo-electron microscopy (cryo-EM) structures of the small-conductance mechanosensitive channel (MscS) in nanodiscs (ND). They reveal a novel membrane-anchoring fold that plays a significant role in channel activation and establish a new location for the lipid bilayer, shifted ~14 Å from previous consensus placements. Two types of lipid densities are explicitly observed. A phospholipid that 'hooks' the top of each TM2-TM3 hairpin and likely plays a role in force sensing, and a bundle of acyl chains occluding the permeation path above the L105 cuff. These observations reshape our understanding of force-from-lipids gating in MscS and highlight the key role of allosteric interactions between TM segments and phospholipids bound to key dynamic components of the channel.

PubMed: 31880537
DOI: 10.7554/eLife.50486

Experimental method

ELECTRON MICROSCOPY (3.4 Å)