4YFR

Crystal structure of the R111K:Y134F:T54V:R132Q:P39Y:R59Y mutant of human Cellular Retinoic Acid Binding Protein II with Retinal at 1.95 Angstrom Resolution - UV irradiated crystal for 30 minutes - 1st Cycle

Summary for 4YFR

• Entry DOI: 10.2210/pdb4yfr/pdb
• Related: 4EEJ 4I9S 4RUU 4YBP 4YBU 4YFP 4YFQ
• Descriptor: Cellular retinoic acid-binding protein 2, RETINAL (3 entities in total)
• Functional Keywords: photo switchable proteins, retinal isomerization, retinal protonated schiff base pka change, protein engineering, transport protein
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: P29373
• Total number of polymer chains: 1
• Total formula weight: 15863.23

Authors

Nosrati, M.,Geiger, J.H. (deposition date: 2015-02-25, release date: 2016-03-02, Last modification date: 2024-10-23)

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 (1.952 Å)