1ky9
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Crystal Structure of DegP (HtrA)
OverviewOverview
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. 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. 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.
About this StructureAbout this Structure
1KY9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine., Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T, Nature. 2002 Mar 28;416(6879):455-9. PMID:11919638
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