Metastable asymmetrical structure of a shaftless V₁ motor.

ABSTRACT: V₁-ATPase is an ATP-driven rotary motor that is composed of a ring-shaped A₃B₃ complex and a central DF shaft. The nucleotide-free A₃B₃ complex of Enterococcus hirae, composed of three identical A₁B₁ heterodimers, showed a unique asymmetrical structure, probably due to the strong binding of the N-terminal barrel domain, which forms a crown structure. Here, we mutated the barrel region to weaken the crown, and performed structural analyses using high-speed atomic force microscopy and x-ray crystallography of the mutant A₃B₃. The nucleotide-free mutant A₃B₃ complex had a more symmetrical open structure than the wild type. Binding of nucleotides produced a closely pa

SUBMITTER: Maruyama S 

PROVIDER: S-EPMC6353620 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature