1qko
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Bacteriorhodopsin is the simplest known photon-driven proton pump and as | + | 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== | ==About this Structure== | ||
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[[Category: Edman, K.]] | [[Category: Edman, K.]] | ||
[[Category: Hajdu, J.]] | [[Category: Hajdu, J.]] | ||
| - | [[Category: Landau, E | + | [[Category: Landau, E M.]] |
[[Category: Neutze, R.]] | [[Category: Neutze, R.]] | ||
[[Category: Nollert, P.]] | [[Category: Nollert, P.]] | ||
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[[Category: retinal protein]] | [[Category: retinal protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:43 2008'' |
Revision as of 12:40, 21 February 2008
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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 as ligand. Known structural/functional Site: . 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
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