Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.
Journal
Cell reports. Physical science
ISSN: 2666-3864
Titre abrégé: Cell Rep Phys Sci
Pays: United States
ID NLM: 101769239
Informations de publication
Date de publication:
18 Aug 2021
18 Aug 2021
Historique:
entrez:
5
5
2022
pubmed:
6
5
2022
medline:
6
5
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35509376
doi: 10.1016/j.xcrp.2021.100512
pmc: PMC9062587
mid: NIHMS1794253
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM118217
Pays : United States
Déclaration de conflit d'intérêts
DECLARATION OF INTERESTS The authors declare no competing interests.
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