ArticlePLoS computational biology2015
Dynamic Allostery of the Catabolite Activator Protein Revealed by Interatomic Forces.
Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Mutagenic Activation of Glutathione Peroxidase-4: Approaches toward Rational Design of Allosteric Drugs.ACS omega · 2022Article
- Structural Energy Landscapes and Plasticity of the Microstates of ApoBiochemistry · 2020Article
- Entropic allostery dominates the phosphorylation-dependent regulation of Syk tyrosine kinase release from immunoreceptor tyrosine-based activation motifs.Protein science : a publication of the Protein Society · 2018Article
- Predicting Protein Dynamics and Allostery Using Multi-Protein Atomic Distance Constraints.Structure (London, England : 1993) · 2017Article
- One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor.Biophysical journal · 2017Article
- Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane.Scientific reports · 2016Article
- Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.Biophysical journal · 2016Article
- NMR Methods to Study Dynamic Allostery.PLoS computational biology · 2016Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Catabolite Activator Protein (CAP) is a showcase example for entropic allostery. For full activation and DNA binding, the homodimeric protein requires the binding of two cyclic AMP (cAMP) molecules in an anti-cooperative manner, the source of which appears to be largely of entropic nature according to previous experimental studies. We here study at atomic detail the allosteric regulation of CAP with Molecular dynamics (MD) simulations. We recover the experimentally observed entropic penalty for the second cAMP binding event with our recently developed force covariance entropy estimator and reveal allosteric communication pathways with Force Distribution Analyses (FDA). Our observations show that CAP binding results in characteristic changes in the interaction pathways connecting the two cAMP allosteric binding sites with each other, as well as with the DNA binding domains. We identified crucial relays in the mostly symmetric allosteric activation network, and suggest point mutants to test this mechanism. Our study suggests inter-residue forces, as opposed to coordinates, as a highly sensitive measure for structural adaptations that, even though minute, can very effectively propagate allosteric signals.
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