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Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7

Karlberg, Tobias LU ; van den Berg, Susanne ; Hammarström, Martin ; Sagemark, Johanna ; Johansson, Ida LU ; Holmberg-Schiavone, Lovisa and Schüler, Herwig LU orcid (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.

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author
; ; ; ; ; and
publishing date
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}},
}