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Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.


ABSTRACT: Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmembrane protein to convert photons of light to an energy-generating proton gradient. The creation and interrogation of a microbial rhodopsin mimic, based on an orthogonal protein system, would illuminate the design elements required to generate new photoactive proteins with novel function. We describe a microbial rhodopsin mimic, created using a small soluble protein as a template, that specifically photoisomerizes all- trans to 13- cis retinal followed by thermal relaxation to the all- trans isomer, mimicking the bacteriorhodopsin photocycle, in a single crystal. The key element for selective isomerization is a tuned steric interaction between the chromophore and protein, similar to that seen in the microbial rhodopsins. It is further demonstrated that a single mutation converts the system to a protein photoswitch without chromophore photoisomerization or conformational change.

SUBMITTER: Ghanbarpour A 

PROVIDER: S-EPMC7358036 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

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Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.

Ghanbarpour Alireza A   Nairat Muath M   Nosrati Meisam M   Santos Elizabeth M EM   Vasileiou Chrysoula C   Dantus Marcos M   Borhan Babak B   Geiger James H JH  

Journal of the American Chemical Society 20190114 4


Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmembrane protein to convert photons of light to an energy-generating proton gradient. The creation and interrogation of a microbial rhodopsin mimic, based on an orthogonal protein system, would illuminate the design elements required to generate new photoactive proteins with novel function. We describe a microbial rhodopsin mimic, created using a small soluble protein as  ...[more]

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