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7E4G

Crystal structure of schizorhodopsin 4

Summary for 7E4G
Entry DOI10.2210/pdb7e4g/pdb
Descriptorschizorhodopsin 4, ZINC ION, SULFATE ION, ... (6 entities in total)
Functional Keywordsrhodopsin, inward proton pump, membrane protein
Biological sourceAsgard group archaeon
Total number of polymer chains3
Total formula weight86365.53
Authors
Shihoya, W.,Nureki, O. (deposition date: 2021-02-12, release date: 2021-02-24, Last modification date: 2024-11-06)
Primary citationHiguchi, A.,Shihoya, W.,Konno, M.,Ikuta, T.,Kandori, H.,Inoue, K.,Nureki, O.
Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping.
Proc.Natl.Acad.Sci.USA, 118:-, 2021
Cited by
PubMed 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 work as light-driven inward H pumps as xenorhodopsins in bacteria. Although E81 plays an essential role in inward H release, the H is not metastably trapped in such a putative H acceptor, unlike the other H pumps. It remains elusive why SzR exhibits different kinetic behaviors in H release. Here, we report the crystal structure of SzR AM_5_00977 at 2.1 Å 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 around the β-ionone ring are essential for color tuning in SzRs. The cytoplasmic parts of transmembrane helices 2, 6, and 7 are shorter than those in the other microbial rhodopsins, and thus E81 is located near the cytosol and easily exposed to the solvent by light-induced structural change. We propose a model of untrapped inward H release; H is released through the water-mediated transport network from the retinal Schiff base to the cytosol by the side of E81. 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.
PubMed: 33790007
DOI: 10.1073/pnas.2016328118
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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