4zrg | pdb_00004zrg

Visual arrestin mutant - R175E

spinqualitylabelsall models 4zrg, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zrg is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CO2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease ARRS_BOVIN Note=S-antigen induces autoimmune uveitis. Function ARRS_BOVIN Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade. Publication Abstract from PubMed Binding mechanism of arrestin requires photoactivation and phosphorylation of the receptor protein rhodopsin, where the receptor bound phosphate groups cause displacement of the long C-tail 'activating' arrestin. Mutation of arginine 175 to glutamic acid (R175E), a central residue in the polar core and previously predicted as the 'phosphosensor' leads to a pre-active arrestin that is able to terminate phototransduction by binding to non-phosphorylated, light-activated rhodopsin. Here, we report the first crystal structure of a R175E mutant arrestin at 2.7 A resolution that reveals significant differences compared to the basal state reported in full-length arrestin structures. These differences comprise disruption of hydrogen bond network in the polar core, and three-element interaction including disordering of several residues in the receptor-binding finger loop and the C-terminus (residues 361-404). Additionally, R175E structure shows a 7.5 degrees rotation of the amino and carboxy-terminal domains relative to each other. Consistent to the biochemical data, our structure suggests an important role of R29 in the initial activation step of C-tail release. Comparison of the crystal structures of basal arrestin and R175E mutant provide insights into the mechanism of arrestin activation, where binding of the receptor likely induces structural changes mimicked as in R175E. Structural evidence for the role of polar core residue Arg175 in arrestin activation.,Granzin J, Stadler A, Cousin A, Schlesinger R, Batra-Safferling R Sci Rep. 2015 Oct 29;5:15808. doi: 10.1038/srep15808. PMID:26510463 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arrestin 3D structures

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