| 研究実績の概要 |
Our recent precise analyses on structural dynamics of bacterial ABC transporter MsbA using HS-AFM show that lipid A/LPS after flipping across inner membrane (IM) remains in the transmembrane domains (TMDs) core of MsbA even in the presence of many ATPase cycles. Bound ATP locks two NBDs in closed conformation for maintaining an outward-facing conformation that facilitates the flipping of lipid A/LPS across IM. ATPase activity of MsbA (ATP→ADP.Pi) may always go on during and after flipping of lipid A/LPS across membrane. When lipid A/LPS is trapped inside TMDs core of MsbA bound ATP, we do not observe the conformational transitions between inward-facing and outward-facing.
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