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          Institute: MPI für Biochemie     Collection: Structure Research (R. Huber)     Display Documents



ID: 39188.0, MPI für Biochemie / Structure Research (R. Huber)
Crystal structure of DegP (HtrA) reveals a new protease- chaperone machine
Authors:Krojer, T.; Garrido-Franco, M.; Huber, R.; Ehrmann, M.; Clausen, T.
Language:English
Date of Publication (YYYY-MM-DD):2002-03-28
Title of Journal:Nature
Journal Abbrev.:Nature
Volume:416
Issue / Number:6879
Start Page:455
End Page:459
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Molecular chaperones and proteases monitor the folded state of other proteins. In addition to recognizing non-native conformations, these quality control factors distinguish substrates that can be refolded from those that need to be degraded(1). To investigate the molecular basis of this process, we have solved the crystal structure of DegP (also known as HtrA), a widely conserved heat shock protein that combines refolding and proteolytic activities(2). The DegP hexamer is formed by staggered association of trimeric rings. The proteolytic sites are located in a central cavity that is only accessible laterally. The mobile side-walls are constructed by twelve PDZ domains, which mediate the opening and closing of the particle and probably the initial binding of substrate. The inner cavity is lined by several hydrophobic patches that may act as docking sites for unfolded polypeptides. In the chaperone conformation, the protease domain of DegP exists in an inactive state, in which substrate binding in addition to catalysis is abolished.
Comment of the Author/Creator:Date: 2002, MAR 28
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Structure Research (Huber)
External Affiliations:Cardiff Univ, Sch Biosci, Cardiff CF10 3US, S Glam, Wales
Identifiers:ISI:000174607800053 [ID No:1]
ISSN:0028-0836 [ID No:2]
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