Proteomics

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Tension mediated mechanical activation and pocket delipidation lead to an analogous MscL channel state

ABSTRACT: We present HDX-MS data of WT and L89W TbMscL to interrogate the mechanism of molecular activation in this mechanosensitive channel.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Mycobacterium Tuberculosis Eai/osdd271

SUBMITTER: Antonio Calabrese  

LAB HEAD: Antonio Calabrese

PROVIDER: PXD021983 | Pride | 2022-06-07

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
WTandL89W.DnX Other
fbsjrau_191022I_HDX_WTbenchristos_09.raw.zip Raw
fbsjrau_191022I_HDX_WTbenchristos_10.raw.zip Raw
fbsjrau_191022I_HDX_WTbenchristos_11.raw.zip Raw
fbsjrau_191022I_HDX_WTbenchristos_14.raw.zip Raw
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Publications

Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state.

Wang Bolin B   Lane Benjamin J BJ   Kapsalis Charalampos C   Ault James R JR   Sobott Frank F   El Mkami Hassane H   Calabrese Antonio N AN   Kalli Antreas C AC   Pliotas Christos C  

Structure (London, England : 1993) 20220104 4

The mechanosensitive ion channel of large conductance MscL gates in response to membrane tension changes. Lipid removal from transmembrane pockets leads to a concerted structural and functional MscL response, but it remains unknown whether there is a correlation between the tension-mediated state and the state derived by pocket delipidation in the absence of tension. Here, we combined pulsed electron paramagnetic resonance spectroscopy and hydrogen-deuterium exchange mass spectrometry, coupled w  ...[more]

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