id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_jafwrbsxmbgkhls3ph2zr44rte	H. Ronald Kaback	Lactose permease: A beautiful chemiosmotic machine	2012	1	.pdf	application/pdf	667	53	45	Department of Physiology, Molecular Biology Institute, University of Molecular Biology Institute, University of California Los Angeles, USA The lactose permease (LacY), a paradigm for membrane transport sugar translocation drives uphill H+ translocation with the generation of ΔμH̃+, the polarity of which depends on the direction of the sugar concentration gradient. binding sites are located primarily in the Nand C-terminal helix sugar and H+ binding have been identified. membrane at the same level as the sugar-binding site. outward-facing conformation, thereby allowing sugar and H+ release features likely explain how LacY catalyzes lactose/H+ symport in both The primary driving force for alternating access is sugar binding and E-mail address: walker@mrc-mbu.cam.ac.uk The F-ATPases, or F1Fo-ATPases, are multisubunit enzyme complexes found in energy transducing membranes in eubacteria, The ATP hydrolase activities of the enzymes from evident in the variety of the symmetries of the membrane bound E-mail address: pn@mb.au.dk journal homepage: www.elsevier.com/locate/bbabio http://www.sciencedirect.com/science/journal/01678809	./cache/work_jafwrbsxmbgkhls3ph2zr44rte.pdf	./txt/work_jafwrbsxmbgkhls3ph2zr44rte.txt