Crystal Structure of CmeB
- Campylobacter jejuni Multidrug Efflux Pump
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Secondary Structure Zoom-in: the Drug-Binding Domain. Polar residues in green; charged res in blue (+) or red (-); uncharged and non-polar in white. Zoom-in: the Proton Relay Network. Original View: Spacefill, Color by Group
Campylobacter jejuni antibiotic-resistance is mediated by multiple mechanisms. CmeB is a homotrimeric, inner-membrane efflux pump that contributes significantly to antibiotic resistance in C. jejuni. The Cme tripartite system consists of the CmeB pump, the CmeA periplasmic adaptor, and the CmeC outer-membrane channel. Each chain has a distinct Drug-Binding Domain (DBD) that opens a channel to bind drugs from the periplasm, and then closes to extrude them up through the pump's central pore. Notice the dangling loop in the center; this loop gates access to the channel. In each protomer, the conserved residues D409, D410, and K935 form a salt-bridge triad, and establish a proton relay network that powers the protein's conformational changes. Structures and Transport Dynamics
of Campylobacter jejuni Multidrug Efflux Pump. Chih-Chia Su et al. Nature Communications (Nature) 5LQ3 (PDB) Next page: Conformational Changes throughout Drug Transport back
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