5lq3

Structures and transport dynamics of the Campylobacter jejuni multidrug efflux pump CmeBStructures and transport dynamics of the Campylobacter jejuni multidrug efflux pump CmeB

Structural highlights 5lq3 is a 6 chain structure with sequence from Campylobacter jejuni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.55Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q0PBE4_CAMJE Publication Abstract from PubMed 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.Multidrug efflux pumps significantly contribute for bacteria resistance to antibiotics. Here the authors present the structure of Campylobacter jejuni CmeB pump combined with functional FRET assays to propose a transport mechanism where each CmeB protomers is functionally independent from the trimer. Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump.,Su CC, Yin L, Kumar N, Dai L, Radhakrishnan A, Bolla JR, Lei HT, Chou TH, Delmar JA, Rajashankar KR, Zhang Q, Shin YK, Yu EW Nat Commun. 2017 Aug 1;8(1):171. doi: 10.1038/s41467-017-00217-z. PMID:28761097 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 5lq3, resolution 3.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image