Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump

Chih-Chia Su, Linxiang Yin, Nitin Kumar, Lei Dai, Abhijith Radhakrishnan, Jani Reddy Bolla, Hsiang-Ting Lei, Tsung-Han Chou, Jared A. Delmar, Kanagalaghatta R. Rajashankar, Qijing Zhang, Yeon-Kyun Shin and Edward W. Yu ()
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Chih-Chia Su: Iowa State University
Linxiang Yin: Iowa State University
Nitin Kumar: Iowa State University
Lei Dai: Iowa State University
Abhijith Radhakrishnan: Iowa State University
Jani Reddy Bolla: Iowa State University
Hsiang-Ting Lei: Iowa State University
Tsung-Han Chou: Iowa State University
Jared A. Delmar: Iowa State University
Kanagalaghatta R. Rajashankar: Cornell University, Argonne National Laboratory
Qijing Zhang: Iowa State University
Yeon-Kyun Shin: Iowa State University
Edward W. Yu: Iowa State University

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract Resistance-nodulation-cell division efflux pumps are integral membrane proteins that catalyze the export of substrates across cell membranes. Within the hydrophobe-amphiphile efflux subfamily, these resistance-nodulation-cell division proteins largely form trimeric efflux pumps. The drug efflux process has been proposed to entail a synchronized motion between subunits of the trimer to advance the transport cycle, leading to the extrusion of drug molecules. Here we use X-ray crystallography and single-molecule fluorescence resonance energy transfer imaging to elucidate the structures and functional dynamics of the Campylobacter jejuni CmeB multidrug efflux pump. We find that the CmeB trimer displays a very unique conformation. A direct observation of transport dynamics in individual CmeB trimers embedded in membrane vesicles indicates that each CmeB subunit undergoes conformational transitions uncoordinated and independent of each other. On the basis of our findings and analyses, we propose a model for transport mechanism where CmeB protomers function independently within the trimer.

Date: 2017
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DOI: 10.1038/s41467-017-00217-z

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