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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Interactions of a bacterial RND transporter with a transmembrane small protein in a lipid environment Dijun Du , Arthur Neuberger , Mona Wu Orr , Catherine E. Newman , Pin-Chia Hsu , Firdaus Samsudin , Andrzej Szewczak-Harris , Leana M. Ramos , Mekdes Debela , Syma Khalid , Gisela Storz , Ben Luisi Structure 28, 625 - 634.e6 DOI: 10.1016/j.str.2020.03.013 Open Access Show Abstract ▼ Abstract: The small protein AcrZ in Escherichia coli interacts with the transmembrane portion of the multidrug efflux pump AcrB and increases resistance of the bacterium to a subset of the antibiotic substrates of that transporter. It is not clear how the physical association of the two proteins selectively changes activity of the pump for defined substrates. Here, we report cryo-EM structures of AcrB and the AcrBZ complex in lipid environments, and comparisons suggest that conformational changes occur in the drug-binding pocket as a result of AcrZ binding. Simulations indicate that cardiolipin preferentially interacts with the AcrBZ complex, due to increased contact surface, and we observe that chloramphenicol sensitivity of bacteria lacking AcrZ is exacerbated when combined with cardiolipin deficiency. Taken together, the data suggest that AcrZ and lipid cooperate to allosterically modulate AcrB activity. This mode of regulation by a small protein and lipid may occur for other membrane proteins.	Jun 2020
Krios I-Titan Krios I at Diamond	Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution Andrzej Szewczak-Harris , James Wagstaff , Jan Lowe Febs Letters DOI: 10.1002/1873-3468.13471 Diamond Proposal Number(s): [17434] Open Access Show Abstract ▼ Abstract: Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z‐ring from assembling anywhere but the mid‐cell, through an oscillatory diffusion‐reaction mechanism. MinD dimers bind to membranes and, via their partner MinC, inhibit the polymerization of cell division protein FtsZ into the Z‐ring. MinC and MinD form polymeric assemblies in solution and on cell membranes. Here, we report the high‐resolution cryo‐EM structure of the copolymeric filaments of Pseudomonas aeruginosa MinCD. The filaments consist of three protofilaments made of alternating MinC and MinD dimers. The MinCD protofilaments are almost completely straight and assemble as single protofilaments on lipid membranes, which we also visualized by cryo‐EM.	Jun 2019

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