1jv7

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(New page: 200px<br /><applet load="1jv7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jv7, resolution 2.25&Aring;" /> '''BACTERIORHODOPSIN O-...)
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[[Image:1jv7.jpg|left|200px]]<br /><applet load="1jv7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jv7, resolution 2.25&Aring;" />
caption="1jv7, resolution 2.25&Aring;" />
'''BACTERIORHODOPSIN O-LIKE INTERMEDIATE STATE OF THE D85S MUTANT AT 2.25 ANGSTROM RESOLUTION'''<br />
'''BACTERIORHODOPSIN O-LIKE INTERMEDIATE STATE OF THE D85S MUTANT AT 2.25 ANGSTROM RESOLUTION'''<br />
==Overview==
==Overview==
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Crystal structures are reported for the D85S and D85S/F219L mutants of the, light-driven proton/hydroxyl-pump bacteriorhodopsin. These mutants, crystallize in the orthorhombic C222(1) spacegroup, and provide the first, demonstration that monoolein-based cubic lipid phase crystallization can, support the growth of well-diffracting crystals in non-hexagonal, spacegroups. Both structures exhibit similar and substantial differences, relative to wild-type bacteriorhodopsin, suggesting that they represent, inherent features resulting from neutralization of the Schiff base, counterion Asp85. We argue that these structures provide a model for the, last photocycle intermediate (O) of bacteriorhodopsin, in which Asp85 is, protonated, the proton release group is deprotonated, and the retinal has, reisomerized to all-trans. Unlike for the M and N photointermediates, where structural changes occur mainly on the cytoplasmic side, here the, large-scale changes are confined to the extracellular side. As in the M, intermediate, the side-chain of Arg82 is in a downward configuration, and, in addition, a pi-cloud hydrogen bond forms between Trp189 NE1 and Trp138., On the cytoplasmic side, there is increased hydration near the surface, suggesting how Asp96 might communicate with the bulk during the rise of, the O intermediate.
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Crystal structures are reported for the D85S and D85S/F219L mutants of the light-driven proton/hydroxyl-pump bacteriorhodopsin. These mutants crystallize in the orthorhombic C222(1) spacegroup, and provide the first demonstration that monoolein-based cubic lipid phase crystallization can support the growth of well-diffracting crystals in non-hexagonal spacegroups. Both structures exhibit similar and substantial differences relative to wild-type bacteriorhodopsin, suggesting that they represent inherent features resulting from neutralization of the Schiff base counterion Asp85. We argue that these structures provide a model for the last photocycle intermediate (O) of bacteriorhodopsin, in which Asp85 is protonated, the proton release group is deprotonated, and the retinal has reisomerized to all-trans. Unlike for the M and N photointermediates, where structural changes occur mainly on the cytoplasmic side, here the large-scale changes are confined to the extracellular side. As in the M intermediate, the side-chain of Arg82 is in a downward configuration, and in addition, a pi-cloud hydrogen bond forms between Trp189 NE1 and Trp138. On the cytoplasmic side, there is increased hydration near the surface, suggesting how Asp96 might communicate with the bulk during the rise of the O intermediate.
==About this Structure==
==About this Structure==
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1JV7 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 RET and LI1 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JV7 OCA].
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1JV7 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=RET:'>RET</scene> and <scene name='pdbligand=LI1:'>LI1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JV7 OCA].
==Reference==
==Reference==
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[[Category: Halobacterium salinarum]]
[[Category: Halobacterium salinarum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cartailler, J.P.]]
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[[Category: Cartailler, J P.]]
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[[Category: Facciotti, M.T.]]
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[[Category: Facciotti, M T.]]
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[[Category: Glaeser, R.M.]]
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[[Category: Glaeser, R M.]]
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[[Category: Lanyi, J.K.]]
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[[Category: Lanyi, J K.]]
[[Category: Luecke, H.]]
[[Category: Luecke, H.]]
[[Category: Needleman, R.]]
[[Category: Needleman, R.]]
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[[Category: photoreceptor]]
[[Category: photoreceptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:36:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:06 2008''

Revision as of 11:27, 21 February 2008


1jv7, resolution 2.25Å

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BACTERIORHODOPSIN O-LIKE INTERMEDIATE STATE OF THE D85S MUTANT AT 2.25 ANGSTROM RESOLUTION

Overview

Crystal structures are reported for the D85S and D85S/F219L mutants of the light-driven proton/hydroxyl-pump bacteriorhodopsin. These mutants crystallize in the orthorhombic C222(1) spacegroup, and provide the first demonstration that monoolein-based cubic lipid phase crystallization can support the growth of well-diffracting crystals in non-hexagonal spacegroups. Both structures exhibit similar and substantial differences relative to wild-type bacteriorhodopsin, suggesting that they represent inherent features resulting from neutralization of the Schiff base counterion Asp85. We argue that these structures provide a model for the last photocycle intermediate (O) of bacteriorhodopsin, in which Asp85 is protonated, the proton release group is deprotonated, and the retinal has reisomerized to all-trans. Unlike for the M and N photointermediates, where structural changes occur mainly on the cytoplasmic side, here the large-scale changes are confined to the extracellular side. As in the M intermediate, the side-chain of Arg82 is in a downward configuration, and in addition, a pi-cloud hydrogen bond forms between Trp189 NE1 and Trp138. On the cytoplasmic side, there is increased hydration near the surface, suggesting how Asp96 might communicate with the bulk during the rise of the O intermediate.

About this Structure

1JV7 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 D85S mutant of bacteriorhodopsin: model of an O-like photocycle intermediate., Rouhani S, Cartailler JP, Facciotti MT, Walian P, Needleman R, Lanyi JK, Glaeser RM, Luecke H, J Mol Biol. 2001 Oct 26;313(3):615-28. PMID:11676543

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