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1x0s
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(New page: 200px<br /><applet load="1x0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x0s, resolution 2.50Å" /> '''Crystal structure of...)
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Revision as of 03:39, 21 November 2007
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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 with SO4, RET, L3P and L2P as ligands. 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 Wed Nov 21 05:46:48 2007
Categories: Halobacterium salinarum | Single protein | Kouyama, T. | Murakami, M. | Nishikawa, T. | L2P | L3P | RET | SO4 | Memebrane protein | Proton pump | Retinal
