ArticleNature communications2025
Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Allosteric gating of radical transport in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductaseProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Measuring multisubunit mechanics of geometrically programmed colloidal assemblies via cryo-EM multi-body refinement.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025Article
- Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.Nature communications · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Understanding the structural dynamics associated with enzymatic catalysis has been a long-standing goal of biochemistry. With the advent of modern cryo-electron microscopy (cryo-EM), it has become conceivable to redefine a protein's structure as the continuum of all conformations and their distributions. However, capturing and interpreting this information remains challenging. Here, we use classification and deep-learning-based analyses to characterize the conformational heterogeneity of a class I ribonucleotide reductase (RNR) during turnover. By converting the resulting information into physically interpretable 2D conformational landscapes, we demonstrate that RNR continuously samples a wide range of motions while maintaining surprising asymmetry to regulate the two halves of its turnover cycle. Remarkably, we directly observe the appearance of highly transient conformations needed for catalysis, as well as the interaction of RNR with its endogenous reductant thioredoxin also contributing to the asymmetry and dynamics of the enzyme complex. Overall, this work highlights the role of conformational dynamics in regulating key steps in enzyme mechanisms.
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