Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 22, Issue 12, Pages 991-998Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3120
Keywords
-
Funding
- Wellcome Trust [WT092552MA]
- Senior Investigator Award [WT100209MA, 093228, 092970]
- Biotechnology and Biological Sciences Research Council [BB/I019855/1, BB/H017917/1, BB/J009784/1]
- Royal Society Wolfson Merit Award
- Engineering and Physical Sciences Research Council Systems Biology Doctoral Training Centre student fellowship
- Biotechnology and Biological Sciences Research Council [BB/H017917/1, BB/I019855/1, BB/H017402/1] Funding Source: researchfish
- BBSRC [BB/H017917/1, BB/H017402/1] Funding Source: UKRI
Ask authors/readers for more resources
The ability of proteins to sense membrane tension is pervasive in biology. A higher-resolution structure of the Escherichia coli small-conductance mechanosensitive channel MscS identifies alkyl chains inside pockets formed by the transmembrane helices (TMs). Purified MscS contains E. coli lipids, and fluorescence quenching demonstrates that phospholipid acyl chains exchange between bilayer and TM pockets. Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chains within them decreases upon channel opening. Phospholipids with one acyl chain per head group (lysolipids) displace normal phospholipids (with two acyl chains) from MscS pockets and trigger channel opening. We propose that the extent of acyl-chain interdigitation in these pockets determines the conformation of MscS. When interdigitation is perturbed by increased membrane tension or by lysolipids, the closed state becomes unstable, and the channel gates.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available