ArticleStructure (London, England : 1993)2016
Characterization of the Domain Orientations of E. coli 5'-Nucleotidase by Fitting an Ensemble of Conformers to DEER Distance Distributions.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025Review
- A novel approach to modeling side chain ensembles of the bifunctional spin label RX.bioRxiv : the preprint server for biology · 2023Article
- Substrate binding modes of purine and pyrimidine nucleotides to human ecto-5'-nucleotidase (CD73) and inhibition by their bisphosphonic acid derivatives.Purinergic signalling · 2021Article
- Benchmark Test and Guidelines for DEER/PELDOR Experiments on Nitroxide-Labeled Biomolecules.Journal of the American Chemical Society · 2021Article
- Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance.Journal of the American Chemical Society · 2021Article
- Methodology for rigorous modeling of protein conformational changes by Rosetta using DEER distance restraints.PLoS computational biology · 2021Article
- Substrate Specificity of Chimeric Enzymes Formed by Interchange of the Catalytic and Specificity Domains of the 5Molecules (Basel, Switzerland) · 2021Article
- Inference of Joint Conformational Distributions from Separately Acquired Experimental Measurements.The journal of physical chemistry letters · 2021Article
- Molecular Dissection ofInternational journal of molecular sciences · 2021Article
- Rapid Simulation of Unprocessed DEER Decay Data for Protein Fold Prediction.Biophysical journal · 2020Article
- Signaling through non-membrane nuclear phosphoinositide binding proteins in human health and disease.Journal of lipid research · 2019Review
- Roles of Phosphorus Sources in Microbial Community Assembly for the Removal of Organic Matters and Ammonia in Activated Sludge.Frontiers in microbiology · 2019Article
- The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018Article
- Natural Conformational Sampling of Human TNFα Visualized by Double Electron-Electron Resonance.Biophysical journal · 2017Article
- Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance.The Journal of biological chemistry · 2017Article
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7 authors.
Funding
Abstract
Escherichia coli 5'-nucleotidase is a two-domain enzyme exhibiting a unique 96° domain motion that is required for catalysis. Here we present an integrated structural biology study that combines DEER distance distributions with structural information from X-ray crystallography and computational biology to describe the population of presumably almost isoenergetic open and closed states in solution. Ensembles of models that best represent the experimental distance distributions are determined by a Monte Carlo search algorithm. As a result, predominantly open conformations are observed in the unliganded state indicating that the majority of enzyme molecules await substrate binding for the catalytic cycle. The addition of a substrate analog yields ensembles with an almost equal mixture of open and closed states. Thus, in the presence of substrate, efficient catalysis is provided by the simultaneous appearance of open conformers (binding substrate or releasing product) and closed conformers (enabling the turnover of the substrate).
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