Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine (Q27638626)

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Michael Ehrmann

object named as

Michael Ehrmann

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Robert Huber

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object named as

Robert Huber

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author name string

Marta Garrido-Franco

Posttranslational quality control: folding, refolding, and degrading proteins.

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language of work or name

English

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publication date

28 March 2002

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published in

Nature

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volume

416

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issue

6879

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page(s)

455-9

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cites work

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

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Protein quality control: triage by chaperones and proteases

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The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase

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The HtrA family of serine proteases

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Primary structure of a putative serine protease specific for IGF-binding proteins

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A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death

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The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins.

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Crystal structure of a PDZ domain

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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

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Crystal structure of heat shock locus V (HslV) from Escherichia coli

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The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis

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Protein translocation channels in the proteasome and other proteases

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A gated channel into the proteasome core particle

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Crystal structure of the tricorn protease reveals a protein disassembly line

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Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ

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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background

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Isolation and characterization of protease Do from Escherichia coli, a large serine protease containing multiple subunits

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Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature

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Structural basis of substrate specificity in the serine proteases

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