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
Link To Document :
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