ArticleNature communications2016
Mass spectrometry locates local and allosteric conformational changes that occur on cofactor binding.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 76 citations in OpenAlex.
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- Viral Receptor-Binding Protein Evolves New Function through Mutations That Cause Trimer Instability and Functional Heterogeneity.Molecular biology and evolution · 2024Article
- Biophysical Characterization of RAS-SOS Complexes by Native Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2024Article
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- Enzymatic Conversion of COChemical reviews · 2023Review
- Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023Review
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- Disassembly Mechanisms and Energetics of Polymetallic Rings and Rotaxanes.Journal of the American Chemical Society · 2022Article
- Gas-Phase Unfolding of Protein Complexes Distinguishes Conformational Isomers.Journal of the American Chemical Society · 2022Article
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Structural mass spectrometry decodes domain interaction and dynamics of the full-length Human Histone Deacetylase 2.Biochimica et biophysica acta. Proteins and proteomics · 2022Article
- Structure and Mechanism ofACS catalysis · 2021Article
- Structural Proteomics Methods to Interrogate the Conformations and Dynamics of Intrinsically Disordered Proteins.Frontiers in chemistry · 2021Review
- Native Mass Spectrometry Can Effectively Predict PROTAC Efficacy.ACS central science · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Fdc1 is a decarboxylase enzyme that requires the novel prenylated FMN cofactor for activity. Here, we use it as an exemplar system to show how native top-down and bottom-up mass spectrometry can measure the structural effect of cofactor binding by a protein. For Fdc1(Ubix), the cofactor confers structural stability to the enzyme. IM-MS shows the holo protein to exist in four closely related conformational families, the populations of which differ in the apo form; the two smaller families are more populated in the presence of the cofactor and depopulated in its absence. These findings, supported by MD simulations, indicate a more open structure for the apo form. HDX-MS reveals that while the dominant structural changes occur proximal to the cofactor-binding site, rearrangements on cofactor binding are evident throughout the protein, predominantly attributable to allosteric conformational tightening, consistent with IM-MS data.
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Registered trials
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.