ArticleThe journal of physical chemistry. B2013
Binding and folding of the small bacterial chaperone HdeA.
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH.Biochimica et biophysica acta. Proteins and proteomics · 2021Article
- Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone.The Journal of biological chemistry · 2019Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- The Mechanism of HdeA Unfolding and Chaperone Activation.Journal of molecular biology · 2018Article
- Optimal allosteric stabilization sites using contact stabilization analysis.Journal of computational chemistry · 2017Article
- Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling.Journal of the American Chemical Society · 2016Article
- Coupled folding and binding with 2D Window-Exchange Umbrella Sampling.Journal of computational chemistry · 2016Article
- HdeB chaperone activity is coupled to its intrinsic dynamic properties.Scientific reports · 2015Article
- Multiscale modeling of a conditionally disordered pH-sensing chaperone.Journal of molecular biology · 2015Article
- Hamiltonian Mapping Revisited: Calibrating Minimalist Models to Capture Molecular Recognition by Intrinsically Disordered Proteins.The journal of physical chemistry letters · 2014Article
- Prepaying the entropic cost for allosteric regulation in KIX.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
3 authors.
Funding
Abstract
The small pH stress-sensing chaperone HdeA helps pathogenic enteric E. coli survive passage through the severely acidic environment of the mammalian stomach. Under stress conditions, HdeA transitions from an inactive folded dimer to a chaperone-active unfolded monomer to prevent the acid-induced aggregation of periplasmic proteins. Here we use a topology-based Gō-like model to delineate the relationship between dimer interface formation and monomer folding and to better understand the structural details of the chaperone activation mechanism. Free energy surfaces show that dimer interface formation and monomer folding proceed concurrently through an on-pathway dimeric intermediate in which one monomer is partially unfolded. The absence of a preexisting fully folded monomer in the proposed binding mechanism is in agreement with HdeA's rapid chaperone response. Binding between unfolded monomers exhibits an enhancement of molecular recognition reminiscent of the fly-casting mechanism. Overall, our simulations further highlight the efficient nature of HdeA's chaperone response and we anticipate that knowledge of a dimeric intermediate will facilitate the interpretation of experimental studies.
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