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 packed spiral-like structure with a disrupted crown. These findings suggest that wild-type A3B3 forms a metastable (stressed) asymmetric structure composed of unstable A1B1 conformers due to the strong constraint of the crown. The results further the understanding of the principle of the cooperative transition mechanism of rotary motors.

journal_name

Sci Adv

journal_title

Science advances

authors

Maruyama S,Suzuki K,Imamura M,Sasaki H,Matsunami H,Mizutani K,Saito Y,Imai FL,Ishizuka-Katsura Y,Kimura-Someya T,Shirouzu M,Uchihashi T,Ando T,Yamato I,Murata T

doi

10.1126/sciadv.aau8149

subject

Has Abstract

pub_date

2019-01-30 00:00:00

pages

eaau8149

issue

1

issn

2375-2548

pii

aau8149

journal_volume

5

pub_type

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