ArticleNature chemistry2014
Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility.
Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 95 citations in OpenAlex.
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- Perspective on the potential of tandem-ion mobility /mass spectrometry methods for structural proteomics applications.Frontiers in analytical science · 2023Article
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- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Cross-linking mass spectrometry uncovers protein interactions and functional assemblies in synaptic vesicle membranes.Nature communications · 2021Article
- Charge Reduction of Membrane Proteins in Native Mass Spectrometry Using Alkali Metal Acetate Salts.Analytical chemistry · 2020Article
- Structural Analysis of the Glycoprotein Complex Avidin by Tandem-Trapped Ion Mobility Spectrometry-Mass Spectrometry (Tandem-TIMS/MS).Analytical chemistry · 2020Article
- Rapid Determination of Activation Energies for Gas-Phase Protein Unfolding and Dissociation in a Q-IM-ToF Mass Spectrometer.Journal of the American Society for Mass Spectrometry · 2020Article
- Integrating hydrogen-deuterium exchange mass spectrometry with molecular dynamics simulations to probe lipid-modulated conformational changes in membrane proteins.Nature protocols · 2019Article
- Untangling Hydrogen Bond Networks with Ion Mobility Spectrometry and Quantum Chemical Calculations: A Case Study on HThe journal of physical chemistry. B · 2019Article
- Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein.Journal of the American Society for Mass Spectrometry · 2018Article
- MgATP hydrolysis destabilizes the interaction between subunit H and yeast VThe Journal of biological chemistry · 2018Article
- Lipids Shape the Electron Acceptor-Binding Site of the Peripheral Membrane Protein Dihydroorotate Dehydrogenase.Cell chemical biology · 2018Article
- Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease.Current opinion in chemical biology · 2018Review
- Characterization of Conformational Ensembles of Protonated N-glycans in the Gas-Phase.Scientific reports · 2018Article
- Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex.Nucleic acids research · 2017Article
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8 authors at 4 institutions in 3 countries.
Funding
Abstract
Rotary ATPases play fundamental roles in energy conversion as their catalytic rotation is associated with interdomain fluctuations and heterogeneity of conformational states. Using ion mobility mass spectrometry we compared the conformational dynamics of the intact ATPase from Thermus thermophilus with those of its membrane and soluble subcomplexes. Our results define regions with enhanced flexibility assigned to distinct subunits within the overall assembly. To provide a structural context for our experimental data we performed molecular dynamics simulations and observed conformational changes of the peripheral stalks that reflect their intrinsic flexibility. By isolating complexes at different phases of cell growth and manipulating nucleotides, metal ions and pH during isolation, we reveal differences that can be related to conformational changes in the Vo complex triggered by ATP binding. Together these results implicate nucleotides in modulating flexibility of the stator components and uncover mechanistic detail that underlies operation and regulation in the context of the holoenzyme.
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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.