1X0S
Crystal structure of the 13-cis isomer of bacteriorhodopsin
Summary for 1X0S
Entry DOI | 10.2210/pdb1x0s/pdb |
Related | 1X0I 1X0K 1iw6 |
Descriptor | Bacteriorhodopsin, beta-D-galactopyranose-(1-6)-alpha-D-mannopyranose-(1-2)-alpha-D-glucopyranose, SULFATE ION, ... (7 entities in total) |
Functional Keywords | proton pump, retinal, memebrane protein, proton transport |
Biological source | Halobacterium salinarum |
Total number of polymer chains | 1 |
Total formula weight | 31893.22 |
Authors | Nishikawa, T.,Murakami, M.,Kouyama, T. (deposition date: 2005-03-28, release date: 2005-08-30, Last modification date: 2024-10-23) |
Primary citation | Nishikawa, T.,Murakami, M.,Kouyama, T. Crystal structure of the 13-cis isomer of bacteriorhodopsin in the dark-adapted state. J.Mol.Biol., 352:319-328, 2005 Cited by PubMed Abstract: 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. PubMed: 16084526DOI: 10.1016/j.jmb.2005.07.021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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