1AP9
X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES
Summary for 1AP9
| Entry DOI | 10.2210/pdb1ap9/pdb |
| Descriptor | BACTERIORHODOPSIN, RETINAL (3 entities in total) |
| Functional Keywords | photoreceptor, proton pump, membrane protein, retinal protein, microcrystals, microfocus beam, lipidic cubic phases |
| Biological source | Halobacterium salinarum |
| Cellular location | Cell membrane; Multi-pass membrane protein: P02945 |
| Total number of polymer chains | 1 |
| Total formula weight | 27098.85 |
| Authors | Pebay-Peyroula, E.,Rummel, G.,Rosenbusch, J.P.,Landau, E.M. (deposition date: 1997-07-26, release date: 1998-09-16, Last modification date: 2024-11-13) |
| Primary citation | Pebay-Peyroula, E.,Rummel, G.,Rosenbusch, J.P.,Landau, E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science, 277:1676-1681, 1997 Cited by PubMed Abstract: Lipidic cubic phases provide a continuous three-dimensional bilayer matrix that facilitates nucleation and growth of bacteriorhodopsin microcrystals. The crystals diffract x-rays isotropically to 2.0 angstroms. The structure of this light-driven proton pump was solved at a resolution of 2.5 angstroms by molecular replacement, using previous results from electron crystallographic studies as a model. The earlier structure was generally confirmed, but several differences were found, including loop conformations and side chain residues. Eight water molecules are now identified experimentally in the proton pathway. These findings reveal the constituents of the proton translocation pathway in the ground state. PubMed: 9287223DOI: 10.1126/science.277.5332.1676 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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