Global structural changes of an ion channel during its gating are followed by ion mobility mass spectrometry

A. Konijnenberg, D. Yilmaz, H.I. Ingólfsson, A. Dimitrova, S.J. Marrink, Z. Li, C. Vénien-Bryan, F. Sobott, A. Kocer

Research output: Contribution to journalArticleAcademicpeer-review

54 Citations (Scopus)

Abstract

Mechanosensitive ion channels are sensors probing membrane tension in all species; despite their importance and vital role in many cell functions, their gating mechanism remains to be elucidated. Here, we determined the conditions for releasing intact mechanosensitive channel of large conductance (MscL) proteins from their detergents in the gas phase using native ion mobility–mass spectrometry (IM-MS). By using IM-MS, we could detect the native mass of MscL from Escherichia coli, determine various global structural changes during its gating by measuring the rotationally averaged collision cross-sections, and show that it can function in the absence of a lipid bilayer. We could detect global conformational changes during MscL gating as small as 3%. Our findings will allow studying native structure of many other membrane proteins.
Original languageEnglish
Pages (from-to)17170-17175
JournalProceedings of the National Academy of Sciences of the United States of America
Volume111
Issue number48
DOIs
Publication statusPublished - 2014
Externally publishedYes

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