Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor

V1-ATPases are rotary molecular motors that are powered by ATP hydrolysis. Here, the authors report two of the missing rotary states of this protein complex, and perform biochemical analysis to investigate the binding mode of the nucleotides.

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Detalles Bibliográficos
Autores principales: Kano Suzuki, Kenji Mizutani, Shintaro Maruyama, Kazumi Shimono, Fabiana L. Imai, Eiro Muneyuki, Yoshimi Kakinuma, Yoshiko Ishizuka-Katsura, Mikako Shirouzu, Shigeyuki Yokoyama, Ichiro Yamato, Takeshi Murata
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/5851f81ae2544c9da73cb1883a72a8dc
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Sumario:V1-ATPases are rotary molecular motors that are powered by ATP hydrolysis. Here, the authors report two of the missing rotary states of this protein complex, and perform biochemical analysis to investigate the binding mode of the nucleotides.