1E12
Halorhodopsin, a light-driven chloride pump
Summary for 1E12
| Entry DOI | 10.2210/pdb1e12/pdb |
| Related | 1BRR |
| Descriptor | HALORHODOPSIN, CHLORIDE ION, POTASSIUM ION, ... (7 entities in total) |
| Functional Keywords | ion pump, chloride pump, membrane protein, retinal protein, lipids, palmitate, haloarchaea, chloride transport, transport protein |
| Biological source | HALOBACTERIUM SALINARUM |
| Total number of polymer chains | 1 |
| Total formula weight | 31127.43 |
| Authors | Essen, L.-O.,Kolbe, M.,Oesterhelt, D. (deposition date: 2000-04-14, release date: 2000-06-02, Last modification date: 2024-10-16) |
| Primary citation | Kolbe, M.,Besir, H.,Essen, L.-O.,Oesterhelt, D. Structure of Light-Driven Chloride Pump Halorhodopsin at 1.8 A Resolution Science, 288:1390-, 2000 Cited by PubMed Abstract: Halorhodopsin, an archaeal rhodopsin ubiquitous in Haloarchaea, uses light energy to pump chloride through biological membranes. Halorhodopsin crystals were grown in a cubic lipidic phase, which allowed the x-ray structure determination of this anion pump at 1.8 angstrom resolution. Halorhodopsin assembles to trimers around a central patch consisting of palmitic acid. Next to the protonated Schiff base between Lys(242) and the isomerizable retinal chromophore, a single chloride ion occupies the transport site. Energetic calculations on chloride binding reveal a combination of ion-ion and ion-dipole interactions for stabilizing the anion 18 angstroms below the membrane surface. Ion dragging across the protonated Schiff base explains why chloride and proton translocation modes are mechanistically equivalent in archaeal rhodopsins. PubMed: 10827943DOI: 10.1126/SCIENCE.288.5470.1390 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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