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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 2.50&Aring;" /> '''Crystal structure of...)
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'''Crystal structure of the 13-cis isomer of bacteriorhodopsin'''<br />
'''Crystal structure of the 13-cis isomer of bacteriorhodopsin'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1X0S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with SO4, RET, L3P and L2P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X0S OCA].
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1X0S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=RET:'>RET</scene>, <scene name='pdbligand=L3P:'>L3P</scene> and <scene name='pdbligand=L2P:'>L2P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X0S OCA].
==Reference==
==Reference==
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[[Category: retinal]]
[[Category: retinal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:46:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:57 2008''

Revision as of 13:49, 21 February 2008

Image:1x0s.gif

1x0s, resolution 2.50Å

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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 , , and 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

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