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

Tobias Krojer, Marta Garrido-Franco, Robert Huber, Michael Ehrmann and Tim Clausen ()
Additional contact information
Tobias Krojer: Max-Planck-Institut für Biochemie, Abteilung Strukturforschung
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

Nature, 2002, vol. 416, issue 6879, 455-459

Abstract: 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.

Date: 2002
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/416455a Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:416:y:2002:i:6879:d:10.1038_416455a

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/416455a

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().