5W0P

Crystal structure of rhodopsin bound to visual arrestin determined by X-ray free electron laser

5W0P の概要

• エントリーDOI: 10.2210/pdb5w0p/pdb
• 関連するPDBエントリー: 4ZWJ
• 分子名称: Endolysin,Rhodopsin,S-arrestin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: rhodopsin, gpcr, arrestin, grk, phosphorylation codes, membrane proteins, signaling protein
• 由来する生物種: Enterobacteria phage RB55; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 405629.81

構造登録者

Zhou, X.E.,He, Y.,de Waal, P.W.,Gao, X.,Kang, Y.,Van Eps, N.,Yin, Y.,Pal, K.,Goswami, D.,White, T.A.,Barty, A.,Latorraca, N.R.,Chapman, H.N.,Hubbell, W.L.,Dror, R.O.,Stevens, R.C.,Cherezov, V.,Gurevich, V.V.,Griffin, P.R.,Ernst, O.P.,Melcher, K.,Xu, H.E. (登録日: 2017-05-31, 公開日: 2017-08-09, 最終更新日: 2024-10-30)

主引用文献

Zhou, X.E.,He, Y.,de Waal, P.W.,Gao, X.,Kang, Y.,Van Eps, N.,Yin, Y.,Pal, K.,Goswami, D.,White, T.A.,Barty, A.,Latorraca, N.R.,Chapman, H.N.,Hubbell, W.L.,Dror, R.O.,Stevens, R.C.,Cherezov, V.,Gurevich, V.V.,Griffin, P.R.,Ernst, O.P.,Melcher, K.,Xu, H.E.
Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors.
Cell, 170:457-469.e13, 2017

PubMed Abstract: G protein-coupled receptors (GPCRs) mediate diverse signaling in part through interaction with arrestins, whose binding promotes receptor internalization and signaling through G protein-independent pathways. High-affinity arrestin binding requires receptor phosphorylation, often at the receptor's C-terminal tail. Here, we report an X-ray free electron laser (XFEL) crystal structure of the rhodopsin-arrestin complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular β sheet with the N-terminal β strands of arrestin. Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338. These two phospho-residues, together with E341, form an extensive network of electrostatic interactions with three positively charged pockets in arrestin in a mode that resembles binding of the phosphorylated vasopressin-2 receptor tail to β-arrestin-1. Based on these observations, we derived and validated a set of phosphorylation codes that serve as a common mechanism for phosphorylation-dependent recruitment of arrestins by GPCRs.

PubMed: 28753425
DOI: 10.1016/j.cell.2017.07.002

実験手法

X-RAY DIFFRACTION (3.013 Å)