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 Advjournal_title
Science advancesauthors
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 Tdoi
10.1126/sciadv.aau8149subject
Has Abstractpub_date
2019-01-30 00:00:00pages
eaau8149issue
1issn
2375-2548pii
aau8149journal_volume
5pub_type
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