Stahlberg, H. and Kutejová, E. and Suda, K. and Wolpensinger, B. and Lustig, A. and Schatz, G. and Engel, A. and Suzuki, C. K.. (1999) Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits. Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, H. 12. pp. 6787-6790.
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Official URL: http://edoc.unibas.ch/dok/A5257677
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Abstract
Lon (or La) is a soluble, homooligomeric ATP-dependent protease. Mass determination and cryoelectron microscopy of pure mitochondrial Lon from Saccharomyces cerevisiae identify Lon as a flexible ring-shaped heptamer. In the presence of ATP or 5'-adenylylimidodiphosphate, most of the rings are symmetric and resemble other ATP-driven machines that mediate folding and degradation of proteins. In the absence of nucleotides, most of the rings are distorted, with two adjacent subunits forming leg-like protrusions. These results suggest that asymmetric conformational changes serve to power processive unfolding and translocation of substrates to the active site of the Lon protease.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel) 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Stahlberg) |
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UniBasel Contributors: | Engel, Andreas H and Stahlberg, Henning |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | National Academy of Sciences |
ISSN: | 0027-8424 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Related URLs: | |
Identification Number: |
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Last Modified: | 08 Jun 2012 06:44 |
Deposited On: | 22 Mar 2012 13:18 |
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