5nc5 | pdb_00005nc5

Crystal structure of AcrBZ in complex with antibiotic puromycin

spinqualitylabelsall models 5nc5, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nc5 is a 8 chain structure with sequence from Escherichia coli, Escherichia coli K-12 and Escherichia coli O157:H7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: D10, D12, DD9, HEX, LMT, PUY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity. Publication Abstract from PubMed Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell envelope. Here we report the near-atomic resolution cryoEM structures of the Escherichia coli AcrAB-TolC multidrug efflux pump in resting and drug transport states, revealing a quaternary structural switch that allosterically couples and synchronizes initial ligand binding with channel opening. Within the transport-activated state, the channel remains open even though the pump cycles through three distinct conformations. Collectively, our data provide a dynamic mechanism for the assembly and operation of the AcrAB-TolC pump. An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump.,Wang Z, Fan G, Hryc CF, Blaza JN, Serysheva II, Schmid MF, Chiu W, Luisi BF, Du D Elife. 2017 Mar 29;6. pii: e24905. doi: 10.7554/eLife.24905. PMID:28355133 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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