Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7
(2009) In PLoS ONE 4(10).- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/5cec389d-eeee-4fd2-98ab-0be9b50e4ba6
- author
- Karlberg, Tobias
LU
; van den Berg, Susanne
; Hammarström, Martin
; Sagemark, Johanna
; Johansson, Ida
LU
; Holmberg-Schiavone, Lovisa
and Schüler, Herwig
LU
- publishing date
- 2009-10-20
- type
- Contribution to journal
- publication status
- published
- keywords
- 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
- in
- PLoS ONE
- volume
- 4
- issue
- 10
- article number
- e6975
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- scopus:70449411716
- pmid:19841671
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0006975
- language
- English
- LU publication?
- no
- id
- 5cec389d-eeee-4fd2-98ab-0be9b50e4ba6
- date added to LUP
- 2024-11-21 18:02:37
- date last changed
- 2025-05-09 17:39:25
@article{5cec389d-eeee-4fd2-98ab-0be9b50e4ba6, abstract = {{<p>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.</p>}}, author = {{Karlberg, Tobias and van den Berg, Susanne and Hammarström, Martin and Sagemark, Johanna and Johansson, Ida and Holmberg-Schiavone, Lovisa and Schüler, Herwig}}, issn = {{1932-6203}}, keywords = {{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}}, language = {{eng}}, month = {{10}}, number = {{10}}, publisher = {{Public Library of Science (PLoS)}}, series = {{PLoS ONE}}, title = {{Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7}}, url = {{http://dx.doi.org/10.1371/journal.pone.0006975}}, doi = {{10.1371/journal.pone.0006975}}, volume = {{4}}, year = {{2009}}, }