Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

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Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)

ID	4531097
Author(s)	Abrahams, Jan Pieter; Leslie, Andrew G. W.; Lutter, René; Walker, John E.
Author(s) at UniBasel	Abrahams, Jan Pieter
Year	1994
Title	Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
Journal	Nature
Volume	370
Number	6491
Pages / Article-Number	621-628
Mesh terms	Science & TechnologyMultidisciplinary SciencesScience & Technology - Other Topics
Abstract	In the crystal structure of bovine mitochondrial F-1-ATPase determined at 2.8 Angstrom resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha(3) beta(3) subassembly relative to an alpha-helical domain of the gamma-subunit.
Publisher	Nature Research
ISSN/ISBN	0028-0836 ; 1476-4687
edoc-URL	https://edoc.unibas.ch/76000/
Full Text on edoc	No
Digital Object Identifier DOI	10.1038/370621a0
ISI-Number	1994PD31000041
Document type (ISI)	Article

28/04/2024

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