ArticleCell reports. Physical science2021
Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.
Article in Cell reports. Physical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Serial X-ray liquidography: multi-dimensional assay framework for exploring biomolecular structural dynamics with microgram quantities.Nature communications · 2024Article
- Projection to extract the perpendicular component (PEPC) method for extracting kinetics from time-resolved data.Structural dynamics (Melville, N.Y.) · 2023Article
- The Role of Transient Intermediate Structures in the Unfolding of the Trp-Cage Fast-Folding Protein: Generating Ensembles from Time-Resolved X-ray Solution Scattering with Genetic Algorithms.The journal of physical chemistry letters · 2023Article
- Light-induced protein structural dynamics in bacteriophytochrome revealed by time-resolved x-ray solution scattering.Science advances · 2022Article
- Determining the charge distribution and the direction of bond cleavage with femtosecond anisotropic x-ray liquidography.Nature communications · 2022Article
- Tracking the ATP-binding response in adenylate kinase in real time.Science advances · 2021Article
- Structural Dynamics of CInternational journal of molecular sciences · 2021Article
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Authors and funding
8 authors.
Funding
Abstract
Molecular switches alterable between two stable states by environmental stimuli, such as light and temperature, offer the potential for controlling biological functions. Here, we report a circular photoswitchable protein complex made of multiple protein molecules that can rapidly and reversibly switch with significant conformational changes. The structural and photochromic properties of photoactive yellow protein (PYP) are harnessed to construct circular oligomer PYPs (coPYPs) of desired sizes. Considering the light-induced N-terminal protrusion of monomer PYP, we expected coPYPs would expand upon irradiation, but time-resolved X-ray scattering data reveal that the late intermediate has a pronounced light-induced contraction motion. This work not only provides an approach to engineering a novel protein-based molecular switch based on circular oligomers of well-known protein units but also demonstrates the importance of characterizing the structural dynamics of designed molecular switches.
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Registered trials
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