3OAX
Crystal structure of bovine rhodopsin with beta-ionone
Summary for 3OAX
| Entry DOI | 10.2210/pdb3oax/pdb |
| Descriptor | Rhodopsin, heptyl 1-thio-beta-D-glucopyranoside, (3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one, ... (13 entities in total) |
| Functional Keywords | 7tm, signaling protein |
| Biological source | Bos taurus (Bovine) |
| Cellular location | Membrane; Multi-pass membrane protein: P02699 |
| Total number of polymer chains | 2 |
| Total formula weight | 85706.19 |
| Authors | Makino, C.L.,Riley, C.K.,Looney, J.,Crouch, R.K.,Okada, T. (deposition date: 2010-08-05, release date: 2011-01-19, Last modification date: 2024-10-30) |
| Primary citation | Makino, C.L.,Riley, C.K.,Looney, J.,Crouch, R.K.,Okada, T. Binding of more than one retinoid to visual opsins Biophys.J., 99:2366-2373, 2010 Cited by PubMed Abstract: Visual opsins bind 11-cis retinal at an orthosteric site to form rhodopsins but increasing evidence suggests that at least some are capable of binding an additional retinoid(s) at a separate, allosteric site(s). Microspectrophotometric measurements on isolated, dark-adapted, salamander photoreceptors indicated that the truncated retinal analog, β-ionone, partitioned into the membranes of green-sensitive rods; however, in blue-sensitive rod outer segments, there was an enhanced uptake of four or more β-ionones per rhodopsin. X-ray crystallography revealed binding of one β-ionone to bovine green-sensitive rod rhodopsin. Cocrystallization only succeeded with extremely high concentrations of β-ionone and binding did not alter the structure of rhodopsin from the inactive state. Salamander green-sensitive rod rhodopsin is also expected to bind β-ionone at sufficiently high concentrations because the binding site is present on its surface. Therefore, both blue- and green-sensitive rod rhodopsins have at least one allosteric binding site for retinoid, but β-ionone binds to the latter type of rhodopsin with low affinity and low efficacy. PubMed: 20923672DOI: 10.1016/j.bpj.2010.08.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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