1c8s
From Proteopedia
(New page: 200px<br /><applet load="1c8s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c8s, resolution 2.00Å" /> '''BACTERIORHODOPSIN D9...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1c8s.gif|left|200px]]<br /><applet load="1c8s" size=" | + | [[Image:1c8s.gif|left|200px]]<br /><applet load="1c8s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c8s, resolution 2.00Å" /> | caption="1c8s, resolution 2.00Å" /> | ||
'''BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE'''<br /> | '''BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures of the Asp96 to Asn mutant of the light-driven proton | + | Crystal structures of the Asp96 to Asn mutant of the light-driven proton pump bacteriorhodopsin and its M photointermediate produced by illumination at ambient temperature have been determined to 1.8 and 2.0 angstroms resolution, respectively. The trapped photoproduct corresponds to the late M state in the transport cycle-that is, after proton transfer to Asp85 and release of a proton to the extracellular membrane surface, but before reprotonation of the deprotonated retinal Schiff base. Its density map describes displacements of side chains near the retinal induced by its photoisomerization to 13-cis,15-anti and an extensive rearrangement of the three-dimensional network of hydrogen-bonded residues and bound water that accounts for the changed pKa values (where Ka is the acid constant) of the Schiff base and Asp85. The structural changes detected suggest the means for conserving energy at the active site and for ensuring the directionality of proton translocation. |
==About this Structure== | ==About this Structure== | ||
| - | 1C8S 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 LI1, SQU and RET as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1C8S 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=LI1:'>LI1</scene>, <scene name='pdbligand=SQU:'>SQU</scene> and <scene name='pdbligand=RET:'>RET</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C8S OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: retinal protein]] | [[Category: retinal protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:36 2008'' |
Revision as of 10:03, 21 February 2008
|
BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE
Overview
Crystal structures of the Asp96 to Asn mutant of the light-driven proton pump bacteriorhodopsin and its M photointermediate produced by illumination at ambient temperature have been determined to 1.8 and 2.0 angstroms resolution, respectively. The trapped photoproduct corresponds to the late M state in the transport cycle-that is, after proton transfer to Asp85 and release of a proton to the extracellular membrane surface, but before reprotonation of the deprotonated retinal Schiff base. Its density map describes displacements of side chains near the retinal induced by its photoisomerization to 13-cis,15-anti and an extensive rearrangement of the three-dimensional network of hydrogen-bonded residues and bound water that accounts for the changed pKa values (where Ka is the acid constant) of the Schiff base and Asp85. The structural changes detected suggest the means for conserving energy at the active site and for ensuring the directionality of proton translocation.
About this Structure
1C8S is a Single protein structure of sequence from Halobacterium salinarum with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution., Luecke H, Schobert B, Richter HT, Cartailler JP, Lanyi JK, Science. 1999 Oct 8;286(5438):255-61. PMID:10514362
Page seeded by OCA on Thu Feb 21 12:03:36 2008
