ArticleBiophysical journal2015
The Complex Energy Landscape of the Protein IscU.
Article in Biophysical journal, 2015. 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, 17 citations in OpenAlex.
- Dynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly.Nature chemical biology · 2026Article
- Bromodomain dimers: A case study of BRD4 and family-wide AlphaFold predictions.Structural dynamics (Melville, N.Y.) · 2026Article
- Article
- From Protein Design to the Energy Landscape of a Cold Unfolding Protein.The journal of physical chemistry. B · 2022Article
- Light from a firefly at temperatures considerably higher and lower than normal.Scientific reports · 2021Article
- A folding reaction at the C-terminal domain drives temperature sensing in TRPM8 channels.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- The cold denaturation of IscU highlights structure-function dualism in marginally stable proteins.Communications chemistry · 2018Article
- NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis.Molecules (Basel, Switzerland) · 2018Review
- Unfolding the Mysteries of Protein Metamorphosis.ACS chemical biology · 2018Review
- Biomolecular NMR: Past and future.Archives of biochemistry and biophysics · 2017Article
- New Techniques for Ancient Proteins: Direct Coupling Analysis Applied on Proteins Involved in Iron Sulfur Cluster Biogenesis.Frontiers in molecular biosciences · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
IscU, the scaffold protein for iron-sulfur (Fe-S) cluster biosynthesis in Escherichia coli, traverses a complex energy landscape during Fe-S cluster synthesis and transfer. Our previous studies showed that IscU populates two interconverting conformational states: one structured (S) and one largely disordered (D). Both states appear to be functionally important because proteins involved in the assembly or transfer of Fe-S clusters have been shown to interact preferentially with either the S or D state of IscU. To characterize the complex structure-energy landscape of IscU, we employed NMR spectroscopy, small-angle x-ray scattering (SAXS), and differential scanning calorimetry. Results obtained for IscU at pH 8.0 show that its S state is maximally populated at 25°C and that heating or cooling converts the protein toward the D state. Results from NMR and DSC indicate that both the heat- and cold-induced S→D transitions are cooperative and two-state. Low-resolution structural information from NMR and SAXS suggests that the structures of the cold-induced and heat-induced D states are similar. Both states exhibit similar (1)H-(15)N HSQC spectra and the same pattern of peptidyl-prolyl peptide bond configurations by NMR, and both appear to be similarly expanded compared with the S state based on analysis of SAXS data. Whereas in other proteins the cold-denatured states have been found to be slightly more compact than the heat-denatured states, these two states occupy similar volumes in IscU.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.