id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_kkta46aprvda3kxuww62zfddua	Gerhard Grüber	ATP synthases from archaea: The beauty of a molecular motor	2014	13	.pdf	application/pdf	13561	1844	56	structural details of individual A1AO ATP synthase subunits as well as synthases from archaea differ in subunit composition and thus in structure and function. V1VO ATPases and F1FO ATP synthases like α/B or β/A shared a considerable sequence identity (20–30%), whereas other smaller subunits did bacterial F1FO ATP synthase (α3:β3:γ:δ:ε:a:b2:cx) it possesses a watersoluble A1 domain, containing the catalytic sites, and an integral membrane AO domain, involved in ion translocation (Fig. 1A). (A–D) Arrangements of the atomic structures of A1AO ATP synthase subunits inside th state 2), a position which compares well with the binding site of the antibiotic, efrapeptin C in the β subunit of F1FO ATP synthases. position to the so-called DELSEED-region of the nucleotide-binding subunit β of the F1FO ATP synthases [60], which also form a disulphide bond The tip of the central stalk in A1AO ATP synthases is made-up by subunit C, which has a funnel shaped structure [51] with a central cavity,	./cache/work_kkta46aprvda3kxuww62zfddua.pdf	./txt/work_kkta46aprvda3kxuww62zfddua.txt