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Article

Axle-less F1-ATPase rotates in the correct direction.

Science (New York, N.Y.) - 15 Feb 2008

Furuike Shou, Hossain Mohammad Delawar, Maki Yasushi, Adachi Kengo, Suzuki Toshiharu, Kohori Ayako, Itoh Hiroyasu, Yoshida Masasuke, Kinosita Kazuhiko

Abstract excerpt

F1-adenosine triphosphatase (ATPase) is an ATP-driven rotary molecular motor in which the central gamma subunit rotates inside a cylinder made of three alpha and three beta subunits alternately arranged. The rotor shaft, an antiparallel alpha-helical coiled coil of the amino and carboxyl termini of the gamma subunit, deeply penetrates the central cavity of the stator cylinder. We truncated the shaft step by step...

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Identifiers

PMID: 18276891
DOI: 10.1126/science.1151343

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Axle-less F1-ATPase rotates in the correct direction.PMID 18276891Read ↗

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ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis.Semantic proximity Read ↗

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A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase.Semantic proximity Read ↗

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