6MQX
Crystal Structure of All-trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E Human Cellular Retinoic Acid Binding Protein II Irradiated with 400 nm Laser (30 seconds) and Subsequently Dark Adapted (25 minutes) at 2.0 Angstrom Resolution
Summary for 6MQX
| Entry DOI | 10.2210/pdb6mqx/pdb |
| Descriptor | Cellular retinoic acid-binding protein 2, GLYCEROL, RETINAL, ... (4 entities in total) |
| Functional Keywords | ilbp, rhodopsin mimic, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 16063.37 |
| Authors | Ghanbarpour, A.,Geiger, J. (deposition date: 2018-10-11, release date: 2019-01-09, Last modification date: 2023-10-11) |
| Primary citation | Ghanbarpour, A.,Nairat, M.,Nosrati, M.,Santos, E.M.,Vasileiou, C.,Dantus, M.,Borhan, B.,Geiger, J.H. Mimicking Microbial Rhodopsin Isomerization in a Single Crystal. J. Am. Chem. Soc., 141:1735-1741, 2019 Cited by PubMed Abstract: Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmembrane protein to convert photons of light to an energy-generating proton gradient. The creation and interrogation of a microbial rhodopsin mimic, based on an orthogonal protein system, would illuminate the design elements required to generate new photoactive proteins with novel function. We describe a microbial rhodopsin mimic, created using a small soluble protein as a template, that specifically photoisomerizes 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 the chromophore and protein, similar to that seen in the microbial rhodopsins. It is further demonstrated that a single mutation converts the system to a protein photoswitch without chromophore photoisomerization or conformational change. PubMed: 30580520DOI: 10.1021/jacs.8b12493 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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