This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1x0s
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1x0s.gif|left|200px]] | + | [[Image:1x0s.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the 13-cis isomer of bacteriorhodopsin''' | + | {{Structure |
| + | |PDB= 1x0s |SIZE=350|CAPTION= <scene name='initialview01'>1x0s</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=L3P:2,3-DI-O-PHYTANLY-3-SN-GLYCERO-1-PHOSPHORYL-3'-SN-GLYCEROL-1'-PHOSPHATE'>L3P</scene> and <scene name='pdbligand=L2P:2,3-DI-PHYTANYL-GLYCEROL'>L2P</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the 13-cis isomer of bacteriorhodopsin''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1X0S is a [ | + | 1X0S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X0S OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the 13-cis isomer of bacteriorhodopsin in the dark-adapted state., Nishikawa T, Murakami M, Kouyama T, J Mol Biol. 2005 Sep 16;352(2):319-28. PMID:[http:// | + | Crystal structure of the 13-cis isomer of bacteriorhodopsin in the dark-adapted state., Nishikawa T, Murakami M, Kouyama T, J Mol Biol. 2005 Sep 16;352(2):319-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16084526 16084526] |
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 24: | Line 33: | ||
[[Category: retinal]] | [[Category: retinal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:03:49 2008'' |
Revision as of 13:03, 20 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the 13-cis isomer of bacteriorhodopsin
Overview
The atomic structure of the trans isomer of bacteriorhodopsin was determined previously by using a 3D crystal belonging to the space group P622. Here, a structure is reported for another isomer with the 13-cis, 15-syn retinal in a dark-adapted crystal. Structural comparison of the two isomers indicates that retinal isomerization around the C13[double bond]C14 and the C15[double bond]N bonds is accompanied by noticeable displacements of a few residues in the vicinity of the retinal Schiff base and small re-arrangement of the hydrogen-bonding network in the proton release channel. On the other hand, aromatic residues surrounding the retinal polyene chain were found to scarcely move during the dark/light adaptation. This result suggests that variation in the structural rigidity within the retinal-binding pocket is one of the important factors ensuring the stereospecific isomerization of retinal.
About this Structure
1X0S is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the 13-cis isomer of bacteriorhodopsin in the dark-adapted state., Nishikawa T, Murakami M, Kouyama T, J Mol Biol. 2005 Sep 16;352(2):319-28. PMID:16084526
Page seeded by OCA on Thu Mar 20 15:03:49 2008
Categories: Halobacterium salinarum | Single protein | Kouyama, T. | Murakami, M. | Nishikawa, T. | L2P | L3P | RET | SO4 | Memebrane protein | Proton pump | Retinal
