Getting to the bottom of the F1-ATPase

Two new crystal structures describe previously unresolved domains of the F 1 sector of ATP synthase. These domains lie at the interface between the transmembrane rotary motor and the rotating subunits of the F 1 domain and are crucial in coupling rotation of the two sectors to ATP synthesis.

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Bibliographische Detailangaben
Veröffentlicht in:	Nature Structural Biology 2000-11, Vol.7 (11), p.1002-1004
1. Verfasser:	Fillingame, Robert H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Cattle Crystallography, X-Ray Escherichia coli - enzymology Life Sciences Macromolecular Substances Membrane Biology Models, Molecular news-and-views Protein Structure Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Proton-Translocating ATPases - chemistry Proton-Translocating ATPases - metabolism Rotation
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Beschreibung
Zusammenfassung:	Two new crystal structures describe previously unresolved domains of the F 1 sector of ATP synthase. These domains lie at the interface between the transmembrane rotary motor and the rotating subunits of the F 1 domain and are crucial in coupling rotation of the two sectors to ATP synthesis.
ISSN:	1072-8368 1545-9993 1545-9985
DOI:	10.1038/80902