Structural highlights
Publication Abstract from PubMed
The light-gated ion channel channelrhodopsin 2 (ChR2) from Chlamydomonas reinhardtii is a major optogenetic tool. Photon absorption starts a well-characterized photocycle, but the structural basis for the regulation of channel opening remains unclear. We present high-resolution structures of ChR2 and the C128T mutant, which has a markedly increased open-state lifetime. The structure reveals two cavities on the intracellular side and two cavities on the extracellular side. They are connected by extended hydrogen-bonding networks involving water molecules and side-chain residues. Central is the retinal Schiff base that controls and synchronizes three gates that separate the cavities. Separate from this network is the DC gate that comprises a water-mediated bond between C128 and D156 and interacts directly with the retinal Schiff base. Comparison with the C128T structure reveals a direct connection of the DC gate to the central gate and suggests how the gating mechanism is affected by subtle tuning of the Schiff base's interactions.
Structural insights into ion conduction by channelrhodopsin 2.,Volkov O, Kovalev K, Polovinkin V, Borshchevskiy V, Bamann C, Astashkin R, Marin E, Popov A, Balandin T, Willbold D, Buldt G, Bamberg E, Gordeliy V Science. 2017 Nov 24;358(6366). pii: 358/6366/eaan8862. doi:, 10.1126/science.aan8862. PMID:29170206[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Volkov O, Kovalev K, Polovinkin V, Borshchevskiy V, Bamann C, Astashkin R, Marin E, Popov A, Balandin T, Willbold D, Buldt G, Bamberg E, Gordeliy V. Structural insights into ion conduction by channelrhodopsin 2. Science. 2017 Nov 24;358(6366). pii: 358/6366/eaan8862. doi:, 10.1126/science.aan8862. PMID:29170206 doi:http://dx.doi.org/10.1126/science.aan8862
