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bioRxiv · 10.1101/2020.07.28.224907

Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping

Higuchi, A.·Shihoya, W.·Konno, M.·Ikuta, T.·Kandori, H.·Inoue, K.·Nureki, O.
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Abstract

Schizorhodopsins (SzRs), a new rhodopsin family identified in Asgard archaea, are phylogenetically located at an intermediate position between type-1 microbial rhodopsins and heliorhodopsins. SzRs reportedly work as light-driven inward H+ pumps, as xenorhodopsin. Here we report the crystal structure of SzR AM_5_00977 at 2.1 [A] resolution. The SzR structure superimposes well on that of bacteriorhodopsin rather than heliorhodopsin, suggesting that SzRs are classified with type-1 rhodopsins. The structure-based mutagenesis study demonstrated that the residues N100 and V103 are essential for color tuning in SzRs. The cytoplasmic parts of transmembrane helices 2, 6, and 7 in SzR are shorter than those in the other microbial rhodopsins. Thus, E81 is located near the cytosol, playing a critical role in the inward H+ release. We suggested the H+ is not metastably trapped in E81 and released through the water-mediated transport network from the retinal Schiff base to the cytosol. Moreover, most residues on the H+ transport pathway are not conserved between SzRs and xenorhodopsins, suggesting that they have entirely different inward H+ release mechanisms.

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Higuchi, A., Shihoya, W., Konno, M., Ikuta, T., Kandori, H., Inoue, K., Nureki, O.. 2020-07-28. Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping. https://doi.org/10.1101/2020.07.28.224907

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