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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 DOI10.2210/pdb6mpk/pdb
DescriptorCellular retinoic acid-binding protein 2, RETINAL, GLYCEROL, ... (4 entities in total)
Functional Keywordsilbp, rhodopsin mimic, lipid binding protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight16155.47
Authors
Ghanbarpour, A.,Geiger, J. (deposition date: 2018-10-07, release date: 2019-01-09, Last modification date: 2024-10-23)
Primary citationGhanbarpour, 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: 30580520
DOI: 10.1021/jacs.8b12493
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.58 Å)
Structure validation

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