5TE3
Crystal structure of Bos taurus opsin at 2.7 Angstrom
Summary for 5TE3
Entry DOI | 10.2210/pdb5te3/pdb |
Related | 5TE5 |
Descriptor | Rhodopsin, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, octyl beta-D-glucopyranoside, ... (6 entities in total) |
Functional Keywords | signaling protein |
Biological source | Bos taurus (Bovine) |
Cellular location | Membrane; Multi-pass membrane protein: P02699 |
Total number of polymer chains | 1 |
Total formula weight | 41362.22 |
Authors | Gulati, S.,Kiser, P.D.,Palczewski, K. (deposition date: 2016-09-20, release date: 2017-03-15, Last modification date: 2023-10-04) |
Primary citation | Gulati, S.,Jastrzebska, B.,Banerjee, S.,Placeres, A.L.,Miszta, P.,Gao, S.,Gunderson, K.,Tochtrop, G.P.,Filipek, S.,Katayama, K.,Kiser, P.D.,Mogi, M.,Stewart, P.L.,Palczewski, K. Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism. Proc. Natl. Acad. Sci. U.S.A., 114:E2608-E2615, 2017 Cited by PubMed Abstract: Vertebrate rhodopsin (Rh) contains 11--retinal as a chromophore to convert light energy into visual signals. On absorption of light, 11--retinal is isomerized to all--retinal, constituting a one-way reaction that activates transducin (G) followed by chromophore release. Here we report that bovine Rh, regenerated instead with a six-carbon-ring retinal chromophore featuring a C=C double bond locked in its conformation (Rh6mr), employs an atypical isomerization mechanism by converting 11- to an 11,13- configuration for prolonged G activation. Time-dependent UV-vis spectroscopy, HPLC, and molecular mechanics analyses revealed an atypical thermal reisomerization of the 11,13- to the 11- configuration on a slow timescale, which enables Rh6mr to function in a photocyclic manner similar to that of microbial Rhs. With this photocyclic behavior, Rh6mr repeatedly recruits and activates G in response to light stimuli, making it an excellent candidate for optogenetic tools based on retinal analog-bound vertebrate Rhs. Overall, these comprehensive structure-function studies unveil a unique photocyclic mechanism of Rh activation by an 11--to-11,13- isomerization. PubMed: 28289214DOI: 10.1073/pnas.1617446114 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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