ArticleNature structural & molecular biology2010
Determinants of structural and functional plasticity of a widely conserved protease chaperone complex.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed.
- It's ok to be outnumbered - sub-stoichiometric modulation of homomeric protein complexes.RSC medicinal chemistry · 2023Review
- An allosteric HTRA1-calpain 2 complex with restricted activation profile.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Computational Design of Novel Allosteric Inhibitors forMolecules (Basel, Switzerland) · 2021Article
- Molecular structure and the role of high-temperature requirement protein 1 in skeletal disorders and cancers.Cell proliferation · 2020Review
- Activation by substoichiometric inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- ThePlant physiology · 2019Article
- Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions.Nature communications · 2017Article
- Determinants of amyloid fibril degradation by the PDZ protease HTRA1.Nature chemical biology · 2015Article
- A Chlamydia trachomatis strain with a chemically generated amino acid substitution (P370L) in the cthtrA gene shows reduced elementary body production.BMC microbiology · 2015Article
- Temperature dependent dynamics of DegP-trimer: A molecular dynamics study.Computational and structural biotechnology journal · 2015Article
- The LA loop as an important regulatory element of the HtrA (DegP) protease from Escherichia coli: structural and functional studies.The Journal of biological chemistry · 2014Article
- Allosteric regulation of serine protease HtrA2 through novel non-canonical substrate binding pocket.PloS one · 2013Article
- The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide.The Journal of biological chemistry · 2012Article
- Plasticity of PDZ domains in ligand recognition and signaling.FEBS letters · 2012Review
- Human high temperature requirement serine protease A1 (HTRA1) degrades tau protein aggregates.The Journal of biological chemistry · 2012Article
- Genetic analysis of 15 protein folding factors and proteases of the Escherichia coli cell envelope.Journal of bacteriology · 2012Article
- Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.Nature structural & molecular biology · 2012Article
- Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.The Journal of biological chemistry · 2011Article
- Recombinant Deg/HtrA proteases from Synechocystis sp. PCC 6803 differ in substrate specificity, biochemical characteristics and mechanism.The Biochemical journal · 2011Article
- Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Channeling of misfolded proteins into repair, assembly or degradation pathways is often mediated by complex and multifunctional cellular factors. Despite detailed structural information, the underlying regulatory mechanisms governing these factors are not well understood. The extracytoplasmic heat-shock factor DegP (HtrA) is a well-suited model for addressing mechanistic issues, as it is regulated by the common mechanisms of allostery and activation by oligomerization. Site-directed mutagenesis combined with refolding and oligomerization studies of chemically denatured DegP revealed how substrates trigger the conversion of the resting conformation into the active conformation. Binding of specific peptides to PDZ domain-1 causes a local rearrangement that is allosterically transmitted to the substrate-binding pocket of the protease domain. This activated state readily assembles into larger oligomeric particles, thus stabilizing the catalytically active form and providing a degradation cavity for protein substrates. The implications of these data for the mechanism of protein quality control are discussed.
Indexed as
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20581826What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.