5ZIL
Crystal structure of bacteriorhodopsin at 1.29 A resolution
Summary for 5ZIL
| Entry DOI | 10.2210/pdb5zil/pdb |
| Descriptor | Bacteriorhodopsin, RETINAL, 2,3-DI-PHYTANYL-GLYCEROL, ... (4 entities in total) |
| Functional Keywords | proton pump, membrane protein, proton transport |
| Biological source | Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) |
| Total number of polymer chains | 1 |
| Total formula weight | 27958.68 |
| Authors | Hasegawa, N.,Jonotsuka, H.,Miki, K.,Takeda, K. (deposition date: 2018-03-16, release date: 2018-10-10, Last modification date: 2024-10-30) |
| Primary citation | Hasegawa, N.,Jonotsuka, H.,Miki, K.,Takeda, K. X-ray structure analysis of bacteriorhodopsin at 1.3 angstrom resolution. Sci Rep, 8:13123-13123, 2018 Cited by PubMed Abstract: Bacteriorhodopsin (bR) of Halobacterium salinarum is a membrane protein that acts as a light-driven proton pump. bR and its homologues have recently been utilized in optogenetics and other applications. Although the structures of those have been reported so far, the resolutions are not sufficient for elucidation of the intrinsic structural features critical to the color tuning and ion pumping properties. Here we report the accurate crystallographic analysis of bR in the ground state. The influence of X-rays was suppressed by collecting the data under a low irradiation dose at 15 K. Consequently, individual atoms could be separately observed in the electron density map at better than 1.3 Å resolution. Residues from Thr5 to Ala233 were continuously constructed in the model. The twist of the retinal polyene was determined to be different from those in the previous models. Two conformations were observed for the proton release region. We discuss the meaning of these fine structural features. PubMed: 30177765DOI: 10.1038/s41598-018-31370-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.29 Å) |
Structure validation
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