5w0p
From Proteopedia
Crystal structure of rhodopsin bound to visual arrestin determined by X-ray free electron laser
Structural highlights
DiseaseOPSD_HUMAN Retinitis punctata albescens;Congenital stationary night blindness;Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. FunctionOPSD_HUMAN Photoreceptor required for image-forming vision at low light intensity (PubMed:8107847, PubMed:7846071). Required for photoreceptor cell viability after birth (PubMed:2215617, PubMed:12566452). Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins (PubMed:8107847, PubMed:28524165, PubMed:26200343, PubMed:28753425). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:28524165, PubMed:26200343).[1] [2] [3] [4] [5] [6] [7] ENLYS_BPT4 Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.[8] ARRS_MOUSE Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (PubMed:9333241, PubMed:16421323). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (PubMed:16421323).[9] [10] Publication Abstract from PubMedG 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 beta sheet with the N-terminal beta 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 beta-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. Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors.,Zhou XE, He Y, de Waal PW, Gao X, Kang Y, Van Eps N, Yin Y, Pal K, Goswami D, White TA, Barty A, Latorraca NR, Chapman HN, Hubbell WL, Dror RO, Stevens RC, Cherezov V, Gurevich VV, Griffin PR, Ernst OP, Melcher K, Xu HE Cell. 2017 Jul 27;170(3):457-469.e13. doi: 10.1016/j.cell.2017.07.002. PMID:28753425[11] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
Categories: Enterobacteria phage RB55 | Homo sapiens | Large Structures | Mus musculus | Barty A | Chapman HN | Cherezov V | Dror RO | Ernst OP | Gao X | Goswami D | Griffin PR | Gurevich VV | He Y | Hubbell WL | Kang Y | Latorraca NR | Melcher K | Pal K | Stevens RC | Van Eps N | White TA | Xu HE | Yin Y | Zhou XE | De Waal PW