Sandbox27
From Proteopedia
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Bacteriorhodopsin
Bacteriorhodopsin is an integral membrane protein used by organisms of the archaea domain, specifically halobacteria. It converts light energy to chemical energy by functioning as a proton pump that creates a proton gradient across the cell membrane. Bacteriorhodopsin subunits typically aggregate into a repeating hexagonal lattice that can cover up to half of the surface area of the cell. Retinal, a ligand found within the protein, changes its conformation upon the absorption of light. This results in a conformational change in the protein, which facilitates the proton pump ([1]).
Structure
The shown in pink represent some of the hydrophobic elements throughout the crystallized structure of bacteriorhodopsin. The , another type of hydrophobic element in the protein, are shown in purple, while the (specifically, alpha-d-glucose, retinal, and 2,10,23-trimethyl-tetracosane) embedded within the protein are displayed in yellow. Image of the 2-chain bacteriorhodopsin crystal structure crystallized from bicelles in archaeon halobacterium salinarum found at 1kme.
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| 1kme, resolution 2.00Å () | |||||||||
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| Ligands: | , , | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contributors: Meenal Datta
