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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bauer, Jacob A. Kutejová, Eva Levdikov, Vladimir M. Ondrovicová, Gabriela Wilson, Keith S. García-Nafría, Javier Blagova, Elena Suzuki, Carolyn K. Wilkinson, Anthony J. |
| Description | Country affiliation: United kingdom Author Affiliation: García-Nafría J ( York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom.) |
| Abstract | ATP-dependent proteases are crucial for cellular homeostasis. By degrading short-lived regulatory proteins, they play an important role in the control of many cellular pathways and, through the degradation of abnormally misfolded proteins, protect the cell from a buildup of aggregates. Disruption or disregulation of mammalian mitochondrial Lon protease leads to severe changes in the cell, linked with carcinogenesis, apoptosis, and necrosis. Here we present the structure of the proteolytic domain of human mitochondrial Lon at 2 A resolution. The fold resembles those of the three previously determined Lon proteolytic domains from Escherichia coli, Methanococcus jannaschii, and Archaeoglobus fulgidus. There are six protomers in the asymmetric unit, four arranged as two dimers. The intersubunit interactions within the two dimers are similar to those between adjacent subunits of the hexameric ring of E. coli Lon, suggesting that the human Lon proteolytic domain also forms hexamers. The active site contains a 3(10) helix attached to the N-terminal end of alpha-helix 2, which leads to the insertion of Asp852 into the active site, as seen in M. jannaschii. Structural considerations make it likely that this conformation is proteolytically inactive. When comparing the intersubunit interactions of human with those of E. coli Lon taken with biochemical data leads us to propose a mechanism relating the formation of Lon oligomers with a conformational shift in the active site region coupled to a movement of a loop in the oligomer interface, converting the proteolytically inactive form seen here to the active one in the E. coli hexamer. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| DOI | 10.1002/pro.376 |
| Journal | Protein Science |
| Issue Number | 5 |
| Volume Number | 19 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 2010-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Protease La Chemistry Metabolism Amino Acid Sequence Catalytic Domain Crystallography, X-ray Models, Molecular Molecular Sequence Data Genetics Protein Conformation Protein Multimerization Protein Subunits Sequence Alignment Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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