Structural highlights
Function
[RABP2_HUMAN] Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.
Publication Abstract from PubMed
Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmem-brane protein to convert photons of light to an energy-generating proton gradient. The creation and interrogation of a microbial rhodop-sin mimic, based on an orthogonal protein system, would illuminate the design elements required to generate new photoactive proteins with novel function. Described is a microbial rhodopsin mimic, created using a small soluble protein as template, that specifically photo-isomerizes 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 chromophore and protein, similar to that seen in the microbial rhodopsins. It is further demonstrated that a single mutation converts the system into a protein photo-switch without chromophore photoisomerization or conformational change.
Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.,Ghanbarpour A, Nairat M, Nosrati M, Santos EM, Vasileiou C, Dantus M, Borhan B, Geiger JH J Am Chem Soc. 2018 Dec 22. doi: 10.1021/jacs.8b12493. PMID:30580520[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghanbarpour A, Nairat M, Nosrati M, Santos EM, Vasileiou C, Dantus M, Borhan B, Geiger JH. Mimicking Microbial Rhodopsin Isomerization in a Single Crystal. J Am Chem Soc. 2018 Dec 22. doi: 10.1021/jacs.8b12493. PMID:30580520 doi:http://dx.doi.org/10.1021/jacs.8b12493
