@article {27330,
	title = {Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels},
	journal = {Nature Structural and Molecular Biology},
	volume = {29},
	number = {6},
	year = {2022},
	note = {Export Date: 06 April 2024; Cited By: 18},
	month = {2022},
	pages = {592 - 603},
	abstract = {Many organisms sense light using rhodopsins, photoreceptive proteins containing a retinal chromophore. Here we report the discovery, structure and biophysical characterization of bestrhodopsins, a microbial rhodopsin subfamily from marine unicellular algae, in which one rhodopsin domain of eight transmembrane helices or, more often, two such domains in tandem, are C-terminally fused to a bestrophin channel. Cryo-EM analysis of a rhodopsin-rhodopsin-bestrophin fusion revealed that it forms a pentameric megacomplex ( 700 kDa) with five rhodopsin pseudodimers surrounding the channel in the center. Bestrhodopsins are metastable and undergo photoconversion between red- and green-absorbing or green- and UVA-absorbing forms in the different variants. The retinal chromophore, in a unique binding pocket, photoisomerizes from all-trans to 11-cis form. Heterologously expressed bestrhodopsin behaves as a light-modulated anion channel. {\textcopyright} 2022, The Author(s), under exclusive licence to Springer Nature America, Inc.},
	url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85132206207\&doi=10.1038\%2fs41594-022-00783-x\&partnerID=40\&md5=7b9998167b0641662705b948ee69156d},
	author = {Rozenberg, A. and Kaczmarczyk, I. and Matzov, D. and Vierock, J. and Nagata, T. and Sugiura, M. and Katayama, K. and Kawasaki, Y. and Konno, M. and Nagasaka, Y. and Aoyama, M. and Das, I. and Pahima, E. and Church, J. and Adam, S. and Borin, V.A. and Chazan, A. and Augustin, S. and Wietek, J. and Dine, J. and Peleg, Y. and Kawanabe, A. and Fujiwara, Y. and Yizhar, O. and Sheves, M. and Schapiro, I. and Furutani, Y. and Kandori, H. and Inoue, K. and Hegemann, P. and B{\'e}j{\`a}, O. and Shalev-Benami, M.}
}
