ArticleScientific reports2017
Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 33 citations in OpenAlex.
- Recent Progress in Solution Structure Studies of Photosynthetic Proteins Using Small-Angle Scattering Methods.Molecules (Basel, Switzerland) · 2023Review
- Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex.Molecular microbiology · 2022Article
- Deuteration Aiming for Neutron Scattering.Biophysics and physicobiology · 2021Article
- Interdomain Flexibility within NADPH Oxidase Suggested by SANS Using LMNG Stealth Carrier.Biophysical journal · 2020Article
- Hiding the Elephant in the Room with Experimental Neutrons.Biophysical journal · 2020Article
- Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering.Biophysical journal · 2020Article
- Examining Membrane Proteins by Neutron Scattering.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering.Biochemistry and biophysics reports · 2017Article
- 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update.Acta crystallographica. Section D, Structural biology · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We present a combination of small-angle neutron scattering, deuterium labelling and contrast variation, temperature activation and fluorescence spectroscopy as a novel approach to obtain time-resolved, structural data individually from macromolecular complexes and their substrates during active biochemical reactions. The approach allowed us to monitor the mechanical unfolding of a green fluorescent protein model substrate by the archaeal AAA+ PAN unfoldase on the sub-minute time scale. Concomitant with the unfolding of its substrate, the PAN complex underwent an energy-dependent transition from a relaxed to a contracted conformation, followed by a slower expansion to its initial state at the end of the reaction. The results support a model in which AAA ATPases unfold their substrates in a reversible power stroke mechanism involving several subunits and demonstrate the general utility of this time-resolved approach for studying the structural molecular kinetics of multiple protein remodelling complexes and their substrates on the sub-minute time scale.
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