SPring-8, the large synchrotron radiation facility

A research group of the University of Tokyo (Group leader: Osamu Nureki, School of Science of the University of Tokyo) succeeded, for the first time in the world, in clarifying the detailed crystal structure of a membrane protein channelrhodopsin (ChR), which is derived from algae and conducts cations intercellularly upon light irradiation (light-gated cation channel). From the results of the crystal structure and electrophysiological analyses, they successfully clarified for the first time in the world the initial response of ChRs and determined the cation conduction pathway of ChRs, which has been controversial among researchers. Currently, this protein is the focus of much attention as a useful tool that can excite certain nerve cells upon light irradiation. The scientists of this group have not only revealed the mechanism by which light energy is converted to energy used for cation conduction, but also provided the fundamental framework for designing effective neurobiological tools using the crystal structure. In this sense, the results are expected to significantly contribute to studies in the fields of neurobiology and neuropathology. The results of this study were published online in the British scientific journal Nature on 23 January 2012.

Publication:
"Crystal structure of channelrhodopsin light-gated cation channel "
Hideaki E. Kato, Feng Zhang, Ofer Yizhar, Charu Ramakrishnan, Tomohiro Nishizawa, Kunio Hirata, Jumpei Ito, Yusuke Aita, Tomoya Tsukazaki, Shigehiko Hayashi, Peter Hegemann, Andrés D. Maturana, Ryuichiro Ishitani, Karl Deisseroth*, Osamu Nureki*(*First Author)
Nature, Published online 22 January 2012