5zih

Crystal structure of the red light-activated channelrhodopsin Chrimson.

spinqualitylabelsall models 5zih, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zih is a 2 chain structure with sequence from Chlamydomonas noctigama and Chlamydomonas reinhardtii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: LYR, OLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8L435_CHLRE Publication Abstract from PubMed Channelrhodopsins are light-activated ion channels that mediate cation permeation across cell membranes upon light absorption. Red-light-activated channelrhodopsins are of particular interest, because red light penetrates deeper into biological tissues and also enables dual-color experiments in combination with blue-light-activated optogenetic tools. Here we report the crystal structure of the most red-shifted channelrhodopsin from the algae Chlamydomonas noctigama, Chrimson, at 2.6 A resolution. Chrimson resembles prokaryotic proton pumps in the retinal binding pocket, while sharing similarity with other channelrhodopsins in the ion-conducting pore. Concomitant mutation analysis identified the structural features that are responsible for Chrimson's red light sensitivity; namely, the protonation of the counterion for the retinal Schiff base, and the polar residue distribution and rigidity of the retinal binding pocket. Based on these mechanistic insights, we engineered ChrimsonSA, a mutant with a maximum activation wavelength red-shifted beyond 605 nm and accelerated closing kinetics. Crystal structure of the red light-activated channelrhodopsin Chrimson.,Oda K, Vierock J, Oishi S, Rodriguez-Rozada S, Taniguchi R, Yamashita K, Wiegert JS, Nishizawa T, Hegemann P, Nureki O Nat Commun. 2018 Sep 26;9(1):3949. doi: 10.1038/s41467-018-06421-9. PMID:30258177 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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