1c8r: Difference between revisions
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==BACTERIORHODOPSIN D96N BR STATE AT 2.0 A RESOLUTION== | ==BACTERIORHODOPSIN D96N BR STATE AT 2.0 A RESOLUTION== | ||
<StructureSection load='1c8r' size='340' side='right' caption='[[1c8r]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1c8r' size='340' side='right'caption='[[1c8r]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c8r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C8R FirstGlance]. <br> | <table><tr><td colspan='2'>[[1c8r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C8R FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/1c8r_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/1c8r_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1c8r" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1c8r" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus halobius ruber klebahn 1919]] | [[Category: Bacillus halobius ruber klebahn 1919]] | ||
[[Category: Large Structures]] | |||
[[Category: Luecke, H]] | [[Category: Luecke, H]] | ||
[[Category: D96n br state]] | [[Category: D96n br state]] | ||
Revision as of 09:36, 10 October 2019
BACTERIORHODOPSIN D96N BR STATE AT 2.0 A RESOLUTIONBACTERIORHODOPSIN D96N BR STATE AT 2.0 A RESOLUTION
Structural highlights
Function[BACR_HALSA] Light-driven proton pump. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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