Abstract | UNLABELLED: 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. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.
|
Authors | Tobias Karlberg, Susanne van den Berg, Martin Hammarström, Johanna Sagemark, Ida Johansson, Lovisa Holmberg-Schiavone, Herwig Schüler |
Journal | PloS one
(PLoS One)
Vol. 4
Issue 10
Pg. e6975
(Oct 20 2009)
ISSN: 1932-6203 [Electronic] United States |
PMID | 19841671
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
|
Chemical References |
- Peptides
- Metalloendopeptidases
- SPG7 protein, human
- m-AAA proteases
- ATPases Associated with Diverse Cellular Activities
|
Topics |
- ATPases Associated with Diverse Cellular Activities
- Amino Acid Motifs
- Amino Acid Sequence
- Binding Sites
- Crystallography, X-Ray
(methods)
- Escherichia coli
(metabolism)
- Humans
- Hydrogen Bonding
- Metalloendopeptidases
(chemistry)
- Molecular Sequence Data
- Peptides
(chemistry)
- Protein Conformation
- Protein Structure, Tertiary
- Sequence Homology, Amino Acid
|