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Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

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  • Tobias Krojer

    (Max-Planck-Institut für Biochemie, Abteilung Strukturforschung
    Cardiff University, School of Biosciences)

  • Marta Garrido-Franco

    (Max-Planck-Institut für Biochemie, Abteilung Strukturforschung)

  • Robert Huber

    (Max-Planck-Institut für Biochemie, Abteilung Strukturforschung)

  • Michael Ehrmann

    (Cardiff University, School of Biosciences)

  • Tim Clausen

    (Max-Planck-Institut für Biochemie, Abteilung Strukturforschung)

Abstract

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 degraded1. 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 activities2. 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.

Suggested Citation

  • Tobias Krojer & Marta Garrido-Franco & Robert Huber & Michael Ehrmann & Tim Clausen, 2002. "Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine," Nature, Nature, vol. 416(6879), pages 455-459, March.
    • Handle: RePEc:nat:nature:v:416:y:2002:i:6879:d:10.1038_416455a
    DOI: 10.1038/416455a
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