1QHJ

X-RAY STRUCTURE OF BACTERIORHODOPSIN GROWN IN LIPIDIC CUBIC PHASES

Summary for 1QHJ

• Entry DOI: 10.2210/pdb1qhj/pdb
• Descriptor: PROTEIN (BACTERIORHODOPSIN), RETINAL, 1,2-[DI-2,6,10,14-TETRAMETHYL-HEXADECAN-16-OXY]-PROPANE, ... (4 entities in total)
• Functional Keywords: photoreceptor, proton pump, membrane protein, retinal protein, lipidic cubic phases, purple membrane, archeal lipids
• Biological source: Halobacterium salinarum
• Cellular location: Cell membrane; Multi-pass membrane protein: P02945
• Total number of polymer chains: 1
• Total formula weight: 32833.27

Authors

Belrhali, H.,Nollert, P.,Royant, A.,Menzel, C.,Rosenbusch, J.P.,Landau, E.M.,Pebay-Peyroula, E. (deposition date: 1999-05-04, release date: 1999-07-21, Last modification date: 2024-10-30)

Primary citation

Belrhali, H.,Nollert, P.,Royant, A.,Menzel, C.,Rosenbusch, J.P.,Landau, E.M.,Pebay-Peyroula, E.
Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution.
Structure Fold.Des., 7:909-917, 1999

PubMed Abstract: Bacteriorhodopsin (bR) from Halobacterium salinarum is a proton pump that converts the energy of light into a proton gradient that drives ATP synthesis. The protein comprises seven transmembrane helices and in vivo is organized into purple patches, in which bR and lipids form a crystalline two-dimensional array. Upon absorption of a photon, retinal, which is covalently bound to Lys216 via a Schiff base, is isomerized to a 13-cis,15-anti configuration. This initiates a sequence of events - the photocycle - during which a proton is transferred from the Schiff base to Asp85, followed by proton release into the extracellular medium and reprotonation from the cytoplasmic side.

PubMed: 10467143
DOI: 10.1016/S0969-2126(99)80118-X

Experimental method

X-RAY DIFFRACTION (1.9 Å)