5ZIH
Crystal structure of the red light-activated channelrhodopsin Chrimson.
Summary for 5ZIH
| Entry DOI | 10.2210/pdb5zih/pdb |
| Descriptor | Sensory opsin A,Chrimson, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total) |
| Functional Keywords | membrane protein, rhodopsin, ion channel |
| Biological source | Chlamydomonas reinhardtii (Chlamydomonas smithii) More |
| Total number of polymer chains | 2 |
| Total formula weight | 84692.57 |
| Authors | Oda, K.,Vierock, J.,Oishi, S.,Taniguchi, R.,Yamashita, K.,Nishizawa, T.,Hegemann, P.,Nureki, O. (deposition date: 2018-03-15, release date: 2018-11-21, Last modification date: 2023-11-22) |
| Primary citation | Oda, K.,Vierock, J.,Oishi, S.,Rodriguez-Rozada, S.,Taniguchi, R.,Yamashita, K.,Wiegert, J.S.,Nishizawa, T.,Hegemann, P.,Nureki, O. Crystal structure of the red light-activated channelrhodopsin Chrimson. Nat Commun, 9:3949-3949, 2018 Cited by PubMed Abstract: 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 Å 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. PubMed: 30258177DOI: 10.1038/s41467-018-06421-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
