4YBP
Crystal structure of the R111K:Y134F:T54V:R132Q:P39Q:R59Y mutant of human cellular retinoic acid binding proteinii with retinal after 24 hour incubation at 1.83 angstrom resolution - thermodynamic product - 1st cycle
Summary for 4YBP
| Entry DOI | 10.2210/pdb4ybp/pdb |
| Related | 2G7B 4I9R 4I9S 4M6S 4M7M 4RUU 4YBU 4YCE 4YCH |
| Descriptor | Cellular retinoic acid-binding protein 2, RETINAL (3 entities in total) |
| Functional Keywords | protein engineering, photo switchable proteins, retinal isomerization, retinal protonated schiff base pka change, 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: 2024-10-23) |
| 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 Cited by 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: 27310917DOI: 10.1021/jacs.6b03681 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.831 Å) |
Structure validation
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