7CLJ
Crystal structure of Thermoplasmatales archaeon heliorhodopsin E108D mutant
Summary for 7CLJ
| Entry DOI | 10.2210/pdb7clj/pdb |
| Descriptor | heliorhodopsin, RETINAL, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total) |
| Functional Keywords | alpha-helical, membrane protein |
| Biological source | Thermoplasmatales archaeon SG8-52-1 |
| Total number of polymer chains | 1 |
| Total formula weight | 35600.87 |
| Authors | Tanaka, T.,Shihoya, W.,Yamashita, K.,Nureki, O. (deposition date: 2020-07-21, release date: 2020-09-02, Last modification date: 2024-10-09) |
| Primary citation | Tanaka, T.,Singh, M.,Shihoya, W.,Yamashita, K.,Kandori, H.,Nureki, O. Structural basis for unique color tuning mechanism in heliorhodopsin. Biochem.Biophys.Res.Commun., 533:262-267, 2020 Cited by PubMed Abstract: Microbial rhodopsins comprise an opsin protein with seven transmembrane helices and a retinal as the chromophore. An all-trans retinal is covalently bonded to a lysine residue through the retinal Schiff base (RSB) and stabilized by a negatively charged counterion. The distance between the RSB and counterion is closely related to the light energy absorption. However, in heliorhodopsin-48C12 (HeR-48C12), while E107 acts as the counterion, E107D mutation exhibits an identical absorption spectrum to the wild-type, suggesting that the distance does not affect its absorption spectra. Here we present the 2.6 Å resolution crystal structure of the Thermoplasmatales archaeon HeR E108D mutant, which also has an identical absorption spectrum to the wild-type. The structure revealed that D108 does not form a hydrogen bond with the RSB, and its counterion interaction becomes weaker. Alternatively, the serine cluster, S78, S112, and S238 form a distinct interaction network around the RSB. The absorption spectra of the E to D and S to A double mutants suggested that S112 influences the spectral shift by compensating for the weaker counterion interaction. Our structural and spectral studies have revealed the unique spectral shift mechanism of HeR and clarified the physicochemical properties of HeRs. PubMed: 32951839DOI: 10.1016/j.bbrc.2020.06.124 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
