Title of article
Crystal Structure of the 13-cis Isomer of Bacteriorhodopsin in the Dark-adapted State
Author/Authors
Taichi Nishikawa، نويسنده , , Midori Murakami، نويسنده , , Tsutomu Kouyama، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2005
Pages
10
From page
319
To page
328
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 C13double bond; length as m-dashC14 and the C15double bond; length as m-dashN 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.
Keywords
proton pump , retinal , stereo-specificity , Isomerization , membrane protein
Journal title
Journal of Molecular Biology
Serial Year
2005
Journal title
Journal of Molecular Biology
Record number
1245331
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