We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Bacteriorhodopsin
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
== Structural highlights == | == Structural highlights == | ||
| - | Br is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. | + | Br is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. The retinal interacts with hydrophobic and aromatic residues. |
== 3D Structures of bacteriorhodopsin == | == 3D Structures of bacteriorhodopsin == | ||
| Line 29: | Line 29: | ||
**[[1qhj]] - HsBr residues 14-261 + phytanyl derivavative + retinal<br /> | **[[1qhj]] - HsBr residues 14-261 + phytanyl derivavative + retinal<br /> | ||
**[[4hwl]] – HsBr + heptane + hexane + retinal<br /> | **[[4hwl]] – HsBr + heptane + hexane + retinal<br /> | ||
| - | **[[4hwl]] – HsBr + decane + hexane + tetradecane + octane + retinal<br /> | ||
**[[1r84]], [[1r2n]] - HsBr residues 1-232 + retinal – NMR<BR /> | **[[1r84]], [[1r2n]] - HsBr residues 1-232 + retinal – NMR<BR /> | ||
**[[1bct]] - HsBr residues 163-231 – NMR<BR /> | **[[1bct]] - HsBr residues 163-231 – NMR<BR /> | ||
Revision as of 07:35, 30 November 2015
Contents |
Function
Bacteriorhodopsin (Br) is a membrane protein in Archaea which moves protons across the cell membrane.
Structural highlights
Br is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. The retinal interacts with hydrophobic and aromatic residues.
3D Structures of bacteriorhodopsin
Updated on 30-November-2015
See Also
References
- ↑ Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU. Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 doi:10.1021/ja904711k
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Wayne Decatur, Jaime Prilusky
