1e0p

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{{Seed}}
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{{STRUCTURE_1e0p| PDB=1e0p | SCENE= }}
{{STRUCTURE_1e0p| PDB=1e0p | SCENE= }}
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'''L INTERMEDIATE OF BACTERIORHODOPSIN'''
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===L INTERMEDIATE OF BACTERIORHODOPSIN===
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==Overview==
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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 Schiff base. The primary proton transfer event would then neutralize these two groups, cancelling their electrostatic attraction and facilitating a relaxation of helix C to a less strained geometry. Reprotonation of the Schiff base by Asp 85 would thereby be impeded, ensuring vectorial proton transport. Structural rearrangements also occur near the protein's surface, aiding proton release to the extracellular medium.
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The line below this paragraph, {{ABSTRACT_PUBMED_10949307}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10949307 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10949307}}
==About this Structure==
==About this Structure==
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[[Category: Retinal protein hydrogen ion transport]]
[[Category: Retinal protein hydrogen ion transport]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:30:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:56:54 2008''

Revision as of 20:57, 30 June 2008

Image:1e0p.png

Template:STRUCTURE 1e0p

L INTERMEDIATE OF BACTERIORHODOPSIN

Template:ABSTRACT PUBMED 10949307

About this Structure

1E0P is a Single protein structure of sequence from Halobacterium salinarum. 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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