Structures of an intact yeast V-ATPase alone and in complex with bacterial effector VopQ

Vacuolar-type ATPase (V-ATPase) is a rotary protein pump involved in proton translocation across various cellular membranes using the energy of ATP hydrolysis. Despite previous studies on bacterial and eukaryotic V-ATPases, information on the intact structure of a eukaryotic V-ATPase is missing. Here we report cryo-EM structures of the intact yeast V-ATPase and this complex bound to a bacterial effector. We reveal the interaction of the elusive regulatory subunit H with its neighboring subunits. Insight for the catalysis mechanism is gained by determining conformations of the catalytic subunits either empty or bound with nucleotides.

New possibility of hydroxyapatites as noble-metal-free catalysts towards complete decomposition of volatile organic compounds

Initially established catalysis mechanism for the decomposition of VOCs on noble-metal-free hydroxyapatite catalysts.

Gold-catalyzed domino cyclization enabling construction of diverse fused azaspiro tetracyclic scaffolds: a cascade catalysis mechanism due to a substrate and counterion

The detailed mechanism and origins of gold-catalyzed domino cyclization to diverse fused azaspiro tetracyclic scaffolds by cooperative dual catalysis and cascade catalysis are systematically studied.