1e0p | pdb_00001e0p
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L INTERMEDIATE OF BACTERIORHODOPSIN
Overview
A wide variety of mechanisms are used to generate a proton-motive, potential across cell membranes, a function lying at the heart of, bioenergetics. Bacteriorhodopsin, the simplest known proton pump, provides, a paradigm for understanding this process. Here we report, at 2.1 A, resolution, the structural changes in bacteriorhodopsin immediately, preceding the primary proton transfer event in its photocycle. The early, structural rearrangements propagate from the protein's core towards the, extracellular surface, disrupting the network of hydrogen-bonded water, molecules that stabilizes helix C in the ground state. Concomitantly, a, bend of this helix enables the negatively charged primary proton acceptor, Asp 85, to approach closer to the positively charged primary proton donor, the ... [(full description)]
About this Structure
1E0P is a [Single protein] structure of sequence from [Halobacterium salinarum] with RET as [ligand]. Full crystallographic information is available from [OCA].
Reference
Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin., Royant A, Edman K, Ursby T, Pebay-Peyroula E, Landau EM, Neutze R, Nature. 2000 Aug 10;406(6796):645-8. PMID:10949307
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