Sandbox27
From Proteopedia
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'''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks! | '''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks! | ||
| - | + | 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 ([http://en.wikipedia.org/wiki/Bacteriorhodopsin]). | |
| - | The <scene name='Sandbox27/Alpha_helices/1'>alpha helices</scene> shown in pink represent some of the hydrophobic elements throughout the crystallized structure of bacteriorhodopsin. The <scene name='Sandbox27/Beta_sheets/1'>beta strands</scene>, another type of hydrophobic element in the protein, are shown in purple, while the <scene name='Sandbox27/Ligands/1'>ligands</scene> embedded within the protein are displayed in yellow. | + | The <scene name='Sandbox27/Alpha_helices/1'>alpha helices</scene> shown in pink represent some of the hydrophobic elements throughout the crystallized structure of bacteriorhodopsin. The <scene name='Sandbox27/Beta_sheets/1'>beta strands</scene>, another type of hydrophobic element in the protein, are shown in purple, while the <scene name='Sandbox27/Ligands/1'>ligands</scene> (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]]. | |
{{STRUCTURE_1kme | PDB=1kme | SCENE= }} | {{STRUCTURE_1kme | PDB=1kme | SCENE= }} | ||
Revision as of 03:11, 4 March 2009
Bacteriorhodopsin
This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!
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]).
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
