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1ky9

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{{STRUCTURE_1ky9| PDB=1ky9 | SCENE= }}
{{STRUCTURE_1ky9| PDB=1ky9 | SCENE= }}
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'''Crystal Structure of DegP (HtrA)'''
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===Crystal Structure of DegP (HtrA)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11919638 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11919638}}
==About this Structure==
==About this Structure==
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Revision as of 08:17, 2 July 2008

Image:1ky9.png

Template:STRUCTURE 1ky9

Crystal Structure of DegP (HtrA)

Template:ABSTRACT PUBMED 11919638

About this Structure

1KY9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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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