1FBB
CRYSTAL STRUCTURE OF NATIVE CONFORMATION OF BACTERIORHODOPSIN
Summary for 1FBB
| Entry DOI | 10.2210/pdb1fbb/pdb |
| Related | 1FBK |
| Descriptor | BACTERIORHODOPSIN, RETINAL (2 entities in total) |
| Functional Keywords | proton pump, membrane protein, retinal protein, two-dimensional crystal electron diffraction, single crystal, proton transport |
| 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 | Subramaniam, S.,Henderson, R. (deposition date: 2000-07-15, release date: 2000-08-09, Last modification date: 2024-11-06) |
| Primary citation | Subramaniam, S.,Henderson, R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature, 406:653-657, 2000 Cited by PubMed Abstract: Bacteriorhodopsin, a membrane protein with a relative molecular mass of 27,000, is a light driven pump which transports protons across the cell membrane of the halophilic organism Halobacterium salinarum. The chromophore retinal is covalently attached to the protein via a protonated Schiff base. Upon illumination, retinal is isomerized. The Schiff base then releases a proton to the extracellular medium, and is subsequently reprotonated from the cytoplasm. An atomic model for bacteriorhodopsin was first determined by Henderson et al, and has been confirmed and extended by work in a number of laboratories in the last few years. Here we present an atomic model for structural changes involved in the vectorial, light-driven transport of protons by bacteriorhodopsin. A 'switch' mechanism ensures the vectorial nature of pumping. First, retinal unbends, triggered by loss of the Schiff base proton, and second, a protein conformational change occurs. This conformational change, which we have determined by electron crystallography at atomic (3.2 A in-plane and 3.6 A vertical) resolution, is largely localized to helices F and G, and provides an 'opening' of the protein to protons on the cytoplasmic side of the membrane. PubMed: 10949309DOI: 10.1038/35020614 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (3.2 Å) |
Structure validation
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