3OAX

Crystal structure of bovine rhodopsin with beta-ionone

3OAX の概要

• エントリーDOI: 10.2210/pdb3oax/pdb
• 分子名称: 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)
• 機能のキーワード: 7tm, signaling protein
• 由来する生物種: Bos taurus (Bovine)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P02699
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85706.19

構造登録者

Makino, C.L.,Riley, C.K.,Looney, J.,Crouch, R.K.,Okada, T. (登録日: 2010-08-05, 公開日: 2011-01-19, 最終更新日: 2024-10-30)

主引用文献

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

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: 20923672
DOI: 10.1016/j.bpj.2010.08.003

実験手法

X-RAY DIFFRACTION (2.6 Å)