6MPK
Crystal Structure of the 13-cis Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E:A32Y Mutant of Human Cellular Retinoic Acid Binding Protein II in the Dark at 1.58 Angstrom Resolution
Summary for 6MPK
Entry DOI | 10.2210/pdb6mpk/pdb |
Descriptor | Cellular retinoic acid-binding protein 2, RETINAL, GLYCEROL, ... (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 | 16155.47 |
Authors | Ghanbarpour, A.,Geiger, J. (deposition date: 2018-10-07, release date: 2019-01-09, Last modification date: 2024-10-23) |
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 (1.58 Å) |
Structure validation
Download full validation report