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Title | Molecular basis of force-from-lipids gating in the mechanosensitive channel MscS. |
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Journal, issue, pages | Elife, Vol. 8, Year 2019 |
Publish date | Dec 27, 2019 |
Authors | Bharat Reddy / Navid Bavi / Allen Lu / Yeonwoo Park / Eduardo Perozo / |
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 ...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. |
External links | Elife / PubMed:31880537 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.1 - 4.1 Å |
Structure data | EMDB-20508, PDB-6pwn: EMDB-20509, PDB-6pwo: EMDB-20510, PDB-6pwp: |
Chemicals | ChemComp-POV: ChemComp-R16: |
Source |
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Keywords | MEMBRANE PROTEIN / MscS / Nanodisc / Mechanosensitive Channel of Small Conductance / Mechanosensitive / Channel / DDM |