Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.

Journal of bacteriology - 1 Feb 2007

Jomaa Ahmad, Damjanovic Daniela, Leong Vivian, Ghirlando Rodolfo, Iwanczyk Jack, Ortega Joaquin

Abstract excerpt

The Escherichia coli DegP protein is an essential periplasmic protein for bacterial survival at high temperatures. DegP has the unusual property of working as a chaperone below 28 degrees C, but efficiently degrading unfolded proteins above 28 degrees C. Monomeric DegP contains a protease domain and two PDZ domains. It oligomerizes into a hexameric cage through the staggered association of trimers. The active...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chromatography, Gel
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Molecular Chaperones

Share to Periplasmic Proteins

Share to Protein Structure, Secondary

Share to Serine Endopeptidases

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 17122339
DOI: 10.1128/JB.01334-06
PMCID: PMC1797295

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.PMID 17122339Read ↗

Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival.Semantic proximity Read ↗

PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease.Semantic proximity Read ↗

Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.Semantic proximity Read ↗

Dispensable PDZ domain of Escherichia coli YaeL essential protease.Semantic proximity Read ↗

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol.Semantic proximity Read ↗

Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis.Semantic proximity Read ↗

The LA loop as an important regulatory element of the HtrA (DegP) protease from Escherichia coli: structural and functional studies.Semantic proximity Read ↗

Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.Semantic proximity Read ↗

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

Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress.Semantic proximity Read ↗

Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture.Semantic proximity Read ↗

Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.