Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5TE3

Crystal structure of Bos taurus opsin at 2.7 Angstrom

Summary for 5TE3
Entry DOI10.2210/pdb5te3/pdb
Related5TE5
DescriptorRhodopsin, 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 Keywordssignaling protein
Biological sourceBos taurus (Bovine)
Cellular locationMembrane; Multi-pass membrane protein: P02699
Total number of polymer chains1
Total formula weight41362.22
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 citationGulati, 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: 28289214
DOI: 10.1073/pnas.1617446114
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

227933

PDB entries from 2024-11-27

PDB statisticsPDBj update infoContact PDBjnumon