Abstract
The bacterial mechanosensitive channel of Small (MscS) conductance responds to membrane tension by opening when the bacterium experiences hypo-osmotic shock conditions to prevent cell lysis [1]. Environmental factors such as cholesterol [2] and cations/anions [3] also affect the gating behaviour of this channel. Here we report an alanine mutagenesis study using both a computational and experimental approach to investigate the interaction of charged protein residues with lipid headgroups. The computational results on the open structure of MscS show that residues K60 and R46 in TM1 helix interact strongly with cardiolipin (CDL, Fig 1A), while in the closed conformation only R46 interacts with cardiolipin (Fig 1B).
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