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

Peptidase activity of the Escherichia coli Hsp31 chaperone.

The Journal of biological chemistry - 15 Apr 2005

Malki Abderrahim, Caldas Thérèse, Abdallah Jad, Kern Renée, Eckey Viola, Kim So Jung, Cha Sun-Shin, Mori Hirotada, Richarme Gilbert

Abstract excerpt

Hsp31, the Escherichia coli hcha gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperature. Its crystal structure reveals a putative Cys(184), His(185), and Asp(213) catalytic triad similar to that of the Pyrococcus horikoshii protease PH1704, suggesting that it should display a proteolytic activity. A preliminary report has shown that Hsp31 has an exceedingly weak proteolytic...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Cations
Share to Chromatography

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine Endopeptidases

Share to Edetic Acid

Share to Histidine

Share to Hydrolysis

Share to Peptide Elongation Factor Tu

Source

Identifiers

PMID: 15550391
DOI: 10.1074/jbc.M408296200

Genes

SDS

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

Peptidase activity of the Escherichia coli Hsp31 chaperone.PMID 15550391Read ↗

Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding.Semantic proximity Read ↗

Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone.Semantic proximity Read ↗

Mutation of GGMP Repeat Segments of Plasmodium falciparum Hsp70-1 Compromises Chaperone Function and Hop Co-Chaperone Binding.Semantic proximity Read ↗

Functional analysis of cysteine residues of the Hok/Gef type I toxins in Escherichia coli.Semantic proximity Read ↗

The contribution of key hydrophobic residues in ecotin to enzyme-inhibitor complex stability.Semantic proximity Read ↗

The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site.Semantic proximity Read ↗

An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties.Semantic proximity Read ↗

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.Semantic proximity Read ↗

A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium.Semantic proximity Read ↗

In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure.Semantic proximity Read ↗

Truncation and heme pocket mutations reduce production of functional catalase HPII in Escherichia coli.Semantic proximity Read ↗

Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30.Semantic proximity Read ↗

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