Determinants of structural and functional plasticity of a widely conserved protease chaperone complex (Q43004118)

12 November 2017

Determinants of structural and functional plasticity of a widely conserved protease chaperone complex (English)

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12 November 2017

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Luitgard Nagel-Steger

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Robert Huber

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Melisa Merdanovic

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Nicolette Mamant

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Michael Meltzer

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Simon Poepsel

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Alexandra Auckenthaler

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Rie Melgaard

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Patrick Hauske

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Anthony R Clarke

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Markus Kaiser

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27 June 2010

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Nature Structural & Molecular Biology

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837-843

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https://scigraph.springernature.com/pub.10.1038/nsmb.1839

12 November 2017

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A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

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Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control

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Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins

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Structural basis for the regulated protease and chaperone function of DegP

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The HtrA Family of Proteases

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Evolution of peptidase diversity

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Binding of proteins to the PDZ domain regulates proteolytic activity of HtrA1 serine protease.

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Role of the PDZ domains in Escherichia coli DegP protein

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

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Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control

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Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli

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Escherichia coli DegP: a structure-driven functional model

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Selectivity profiling of DegP substrates and inhibitors

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Structural basis of substrate specificity in the serine proteases

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Serine protease mechanism and specificity

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Allosteric regulation of proteases

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Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases

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Identifiers

DOI

10.1038/NSMB.1839

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12 November 2017

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