Title |
Crystal Structure of the ATPase Domain of the Human AAA+ Protein Paraplegin/SPG7
|
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Published in |
PLOS ONE, October 2009
|
DOI | 10.1371/journal.pone.0006975 |
Pubmed ID | |
Authors |
Tobias Karlberg, Susanne van den Berg, Martin Hammarström, Johanna Sagemark, Ida Johansson, Lovisa Holmberg-Schiavone, Herwig Schüler |
Abstract |
Paraplegin is an m-AAA protease of the mitochondrial inner membrane that is linked to hereditary spastic paraplegias. The gene encodes an FtsH-homology protease domain in tandem with an AAA+ homology ATPase domain. The protein is believed to form a hexamer that uses ATPase-driven conformational changes in its AAA-domain to deliver substrate peptides to its protease domain. We present the crystal structure of the AAA-domain of human paraplegin bound to ADP at 2.2 A. This enables assignment of the roles of specific side chains within the catalytic cycle, and provides the structural basis for understanding the mechanism of disease mutations. |
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Readers by professional status | Count | As % |
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Researcher | 17 | 25% |
Student > Ph. D. Student | 13 | 19% |
Student > Master | 6 | 9% |
Unspecified | 5 | 7% |
Student > Bachelor | 5 | 7% |
Other | 16 | 24% |
Unknown | 6 | 9% |
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Unspecified | 5 | 7% |
Other | 7 | 10% |
Unknown | 6 | 9% |