ArticleProceedings of the National Academy of Sciences of the United States of America2013
Global structural motions from the strain of a single hydrogen bond.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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, 42 citations in OpenAlex.
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Energetics and dynamics of the proton shuttle of carbonic anhydrase II.Cellular and molecular life sciences : CMLS · 2023Article
- A Short Tale of the Origin of Proteins and Ribosome Evolution.Microorganisms · 2022Review
- Computational Insights into the Unfolding of a Destabilized Superoxide Dismutase 1 Mutant.Biology · 2021Article
- Article
- Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.eLife · 2020Article
- Diffusive protein interactions in human versus bacterial cells.Current research in structural biology · 2020Article
- Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants.Frontiers in neurology · 2019Review
- Resolving distinct molecular origins for copper effects on PAI-1.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Computing disease-linked SOD1 mutations: deciphering protein stability and patient-phenotype relations.Scientific reports · 2017Article
- Physicochemical code for quinary protein interactions inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- As Simple As Possible, but Not Simpler: Exploring the Fidelity of Coarse-Grained Protein Models for Simulated Force Spectroscopy.PLoS computational biology · 2016Article
- Thermodynamics of protein destabilization in live cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- SOD1 aggregation in ALS mice shows simplistic test tube behavior.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Interaction between dimer interface residues of native and mutated SOD1 protein: a theoretical study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Novel microscale approaches for easy, rapid determination of protein stability in academic and commercial settings.Biochimica et biophysica acta · 2014Article
- Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.The Journal of biological chemistry · 2014Article
- Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Identification of allosteric disulfides from prestress analysis.Biophysical journal · 2014Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The origin and biological role of dynamic motions of folded enzymes is not yet fully understood. In this study, we examine the molecular determinants for the dynamic motions within the β-barrel of superoxide dismutase 1 (SOD1), which previously were implicated in allosteric regulation of protein maturation and also pathological misfolding in the neurodegenerative disease amyotrophic lateral sclerosis. Relaxation-dispersion NMR, hydrogen/deuterium exchange, and crystallographic data show that the dynamic motions are induced by the buried H43 side chain, which connects the backbones of the Cu ligand H120 and T39 by a hydrogen-bond linkage through the hydrophobic core. The functional role of this highly conserved H120-H43-T39 linkage is to strain H120 into the correct geometry for Cu binding. Upon elimination of the strain by mutation H43F, the apo protein relaxes through hydrogen-bond swapping into a more stable structure and the dynamic motions freeze out completely. At the same time, the holo protein becomes energetically penalized because the twisting back of H120 into Cu-bound geometry leads to burial of an unmatched backbone carbonyl group. The question then is whether this coupling between metal binding and global structural motions in the SOD1 molecule is an adverse side effect of evolving viable Cu coordination or plays a key role in allosteric regulation of biological function, or both?
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