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Article

Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel.

Nature structural & molecular biology - 1 Feb 2005

Edwards Michelle D, Li Yuezhou, Kim Sanguk, Miller Samantha, Bartlett Wendy, Black Susan, Dennison Sally, Iscla Irene, Blount Paul, Bowie James U, Booth Ian R

Abstract excerpt

The crystal structure of an open form of the Escherichia coli MscS mechanosensitive channel was recently solved. However, the conformation of the closed state and the gating transition remain uncharacterized. The pore-lining transmembrane helix contains a conserved glycine- and alanine-rich motif that forms a helix-helix interface. We show that introducing 'knobs' on the smooth glycine face by replacing glycine...

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PMID: 15665866
DOI: 10.1038/nsmb895

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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