4YBU

Crystal structure of the R111K:Y134F:T54V:R132Q:P39Q:R59Y mutant of human Cellular Retinoic Acid Binding ProteinII in complex with Retinal after 24 h incubation and 1 hour UV irradiation at 1.92 angstrom - 1st cycle

Summary for 4YBU

• Entry DOI: 10.2210/pdb4ybu/pdb
• Related: 2G7B 4EEJ 4I9R 4I9S 4RUU 4YBP
• Descriptor: Cellular retinoic acid-binding protein 2, RETINAL (3 entities in total)
• Functional Keywords: photoswitchable protein, retinal isomerization, retinal psb, protein engineering, retinal iminium pka change by isomerization, transport protein
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: P29373
• Total number of polymer chains: 1
• Total formula weight: 15828.18

Authors

Nosrati, M.,Geiger, J.H. (deposition date: 2015-02-19, release date: 2016-02-24, Last modification date: 2024-10-16)

Primary citation

Nosrati, M.,Berbasova, T.,Vasileiou, C.,Borhan, B.,Geiger, J.H.
A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution.
J.Am.Chem.Soc., 138:8802-8808, 2016

PubMed Abstract: The members of the rhodopsin family of proteins are involved in many essential light-dependent processes in biology. Specific photoisomerization of the protein-bound retinylidene PSB at a specified wavelength range of light is at the heart of all of these systems. Nonetheless, it has been difficult to reproduce in an engineered system. We have developed rhodopsin mimics, using intracellular lipid binding protein family members as scaffolds, to study fundamental aspects of protein/chromophore interactions. Herein we describe a system that specifically isomerizes the retinylidene protonated Schiff base both thermally and photochemically. This isomerization has been characterized at atomic resolution by quantitatively interconverting the isomers in the crystal both thermally and photochemically. This event is accompanied by a large pKa change of the imine similar to the pKa changes observed in bacteriorhodopsin and visual opsins during isomerization.

PubMed: 27310917
DOI: 10.1021/jacs.6b03681

Experimental method

X-RAY DIFFRACTION (1.924 Å)