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

Karlberg T, van den Berg S, Hammarström M, Sagemark J, Johansson I, Holmberg-Schiavone L, Schüler H - PLoS ONE (2009)

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Affiliation: Structural Genomics Consortium, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.

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.

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The nucleotide binding site of paraplegin.Details of side chain interactions with ADP.
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pone-0006975-g004: The nucleotide binding site of paraplegin.Details of side chain interactions with ADP.

Mentions: The nucleotide binding pocket is located at the interface between the β-sheet and the α-helical bundle (Figure 3). Despite high concentrations of ATP and Mg2+ during crystallization, ADP was clearly seen in the electron density, and as in previously determined FtsH structures [17], density for a magnesium ion was not observed. ADP interacts with side chains from both the amino-terminal part of the AAA-domain and the carboxy-terminal α-helical bundle (Figure 4 and Supplementary Datapack S1).


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

Karlberg T, van den Berg S, Hammarström M, Sagemark J, Johansson I, Holmberg-Schiavone L, Schüler H - PLoS ONE (2009)

The nucleotide binding site of paraplegin.Details of side chain interactions with ADP.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2734466&req=5

pone-0006975-g004: The nucleotide binding site of paraplegin.Details of side chain interactions with ADP.
Mentions: The nucleotide binding pocket is located at the interface between the β-sheet and the α-helical bundle (Figure 3). Despite high concentrations of ATP and Mg2+ during crystallization, ADP was clearly seen in the electron density, and as in previously determined FtsH structures [17], density for a magnesium ion was not observed. ADP interacts with side chains from both the amino-terminal part of the AAA-domain and the carboxy-terminal α-helical bundle (Figure 4 and Supplementary Datapack S1).

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Structural Genomics Consortium, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.

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.

Show MeSH
Related in: MedlinePlus