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1jv6
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Categories: Halobacterium salinarum | Single protein | Cartailler, J P. | Facciotti, M T. | Glaeser, R M. | Lanyi, J K. | Luecke, H. | Needleman, R. | Rouhani, S. | Walian, P. | LI1 | RET | 7-transmembrane | Cubic lipid phase | F219l mutant | Haloarchaea | Ion transport | Photoreceptor
(New page: 200px<br /><applet load="1jv6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jv6, resolution 2.00Å" /> '''BACTERIORHODOPSIN D8...) |
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| - | [[Image:1jv6.jpg|left|200px]]<br /><applet load="1jv6" size=" | + | [[Image:1jv6.jpg|left|200px]]<br /><applet load="1jv6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jv6, resolution 2.00Å" /> | caption="1jv6, resolution 2.00Å" /> | ||
'''BACTERIORHODOPSIN D85S/F219L DOUBLE MUTANT AT 2.00 ANGSTROM RESOLUTION'''<br /> | '''BACTERIORHODOPSIN D85S/F219L DOUBLE MUTANT AT 2.00 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures are reported for the D85S and D85S/F219L mutants of the | + | 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== | ||
| - | 1JV6 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:// | + | 1JV6 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=1JV6 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cartailler, J | + | [[Category: Cartailler, J P.]] |
| - | [[Category: Facciotti, M | + | [[Category: Facciotti, M T.]] |
| - | [[Category: Glaeser, R | + | [[Category: Glaeser, R M.]] |
| - | [[Category: Lanyi, J | + | [[Category: Lanyi, J K.]] |
[[Category: Luecke, H.]] | [[Category: Luecke, H.]] | ||
[[Category: Needleman, R.]] | [[Category: Needleman, R.]] | ||
| Line 30: | Line 30: | ||
[[Category: photoreceptor]] | [[Category: photoreceptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:08 2008'' |
Revision as of 11:27, 21 February 2008
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BACTERIORHODOPSIN D85S/F219L DOUBLE MUTANT AT 2.00 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
1JV6 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
Page seeded by OCA on Thu Feb 21 13:27:08 2008