1qko
From Proteopedia
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HIGH RESOLUTION X-RAY STRUCTURE OF AN EARLY INTERMEDIATE IN THE BACTERIORHODOPSIN PHOTOCYCLE
Overview
Bacteriorhodopsin is the simplest known photon-driven proton pump and as, such provides a model for the study of a basic function in bioenergetics., Its seven transmembrane helices encompass a proton translocation pathway, containing the chromophore, a retinal molecule covalently bound to lysine, 216 through a protonated Schiff base, and a series of proton donors and, acceptors. Photoisomerization of the all-trans retinal to the 13-cis, configuration initiates the vectorial translocation of a proton from the, Schiff base, the primary proton donor, to the extracellular side, followed, by reprotonation of the Schiff base from the cytoplasm. Here we describe, the high-resolution X-ray structure of an early intermediate in the, photocycle of bacteriorhodopsin, which is formed directly after, photoexcitation. A key water molecule is dislocated, allowing the primary, proton acceptor, Asp 85, to move. Movement of the main-chain Lys 216, locally disrupts the hydrogen-bonding network of helix G, facilitating, structural changes later in the photocycle.
About this Structure
1QKO is a Single protein structure of sequence from Halobacterium salinarum with RET as ligand. Structure known Active Site: SFF. Full crystallographic information is available from OCA.
Reference
High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle., Edman K, Nollert P, Royant A, Belrhali H, Pebay-Peyroula E, Hajdu J, Neutze R, Landau EM, Nature. 1999 Oct 21;401(6755):822-6. PMID:10548112
Page seeded by OCA on Mon Nov 5 17:01:17 2007
