5W0P

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

Summary for 5W0P

• Entry DOI: 10.2210/pdb5w0p/pdb
• Related: 4ZWJ
• Descriptor: Endolysin,Rhodopsin,S-arrestin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: rhodopsin, gpcr, arrestin, grk, phosphorylation codes, membrane proteins, signaling protein
• Biological source: Enterobacteria phage RB55; More
• Total number of polymer chains: 4
• Total formula weight: 405629.81

Authors

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. (deposition date: 2017-05-31, release date: 2017-08-09, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.013 Å)