ArticleMolecular cell2011
Structural instability tuning as a regulatory mechanism in protein-protein interactions.
Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- An optimizedJournal of biomolecular NMR · 2025Article
- Mechanisms of assembly and function of the Hsp70-Hsp40 chaperone machinery.Molecular cell · 2025Article
- Remote on-off switching of protein activity by intrinsically disordered region.Nature structural & molecular biology · 2025Article
- The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception.Molecules (Basel, Switzerland) · 2022Review
- Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins.Microorganisms · 2021Review
- A Reporter System for Fast Quantitative Monitoring of Type 3 Protein Secretion in EnteropathogenicMicroorganisms · 2020Article
- Conformational states dynamically populated by a kinase determine its function.Science (New York, N.Y.) · 2020Article
- Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system.Nature communications · 2018Article
- Large-scale production of a thermostable Rhodothermus marinus cellulase by heterologous secretion from Streptomyces lividans.Microbial cell factories · 2017Article
- Hierarchical protein targeting and secretion is controlled by an affinity switch in the type III secretion system of enteropathogenicThe EMBO journal · 2017Article
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
- Nuclear Magnetic Resonance Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa.Biochemistry · 2015Article
- The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded.Journal of molecular biology · 2015Article
- Energy landscapes of functional proteins are inherently risky.Nature chemical biology · 2014Article
- Structural basis for protein antiaggregation activity of the trigger factor chaperone.Science (New York, N.Y.) · 2014Article
- NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.Physical chemistry chemical physics : PCCP · 2014Article
- Article
- Regulated structural transitions unleash the chaperone activity of αB-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Allosteric inhibition through suppression of transient conformational states.Nature chemical biology · 2013Article
- Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion.Cell reports · 2013Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Protein-protein interactions mediate a vast number of cellular processes. Here, we present a regulatory mechanism in protein-protein interactions mediated by finely tuned structural instability and coupled with molecular mimicry. We show that a set of type III secretion (TTS) autoinhibited homodimeric chaperones adopt a molten globule-like state that transiently exposes the substrate binding site as a means to become rapidly poised for binding to their cognate protein substrates. Packing defects at the homodimeric interface stimulate binding, whereas correction of these defects results in less labile chaperones that give rise to nonfunctional biological systems. The protein substrates use structural mimicry to offset the weak spots in the chaperones and to counteract their autoinhibitory conformation. This regulatory mechanism of protein activity is evolutionarily conserved among several TSS systems and presents a lucid example of functional advantage conferred upon a biological system by finely tuned structural instability.
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