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4ygg

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CRYSTAL STRUCTURE OF R111K:Y134F:T54V:R132Q:P39Y:R59Y MUTANT OF HUMAN CELLULAR RETINOIC ACID BINDING PROTEIN II WITH RETINAL AT 1.9 ANGSTROM RESOLUTION - VISIBLE LIGHT IRRADIATED CRYSTAL - 2ND CYCLE

Structural highlights

4ygg is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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.

A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution.,Nosrati M, Berbasova T, Vasileiou C, Borhan B, Geiger JH J Am Chem Soc. 2016 Jul 5. PMID:27310917^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nosrati M, Berbasova T, Vasileiou C, Borhan B, Geiger JH. A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution. J Am Chem Soc. 2016 Jul 5. PMID:27310917 doi:http://dx.doi.org/10.1021/jacs.6b03681