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==Crystal structure of bacteriorhodopsin mutant L94A crystallized from bicelles==
==Crystal structure of bacteriorhodopsin mutant L94A crystallized from bicelles==
<StructureSection load='3hao' size='340' side='right' caption='[[3hao]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
<StructureSection load='3hao' size='340' side='right'caption='[[3hao]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hao]] is a 2 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=3HAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HAO FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hao]] is a 2 chain structure with sequence from [https://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=3HAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HAO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3han|3han]], [[3hap|3hap]], [[3haq|3haq]], [[3har|3har]], [[3has|3has]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3han|3han]], [[3hap|3hap]], [[3haq|3haq]], [[3har|3har]], [[3has|3has]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bop, VNG_1467G ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 "Bacillus halobius ruber" Klebahn 1919])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bop, VNG_1467G ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 "Bacillus halobius ruber" Klebahn 1919])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hao OCA], [http://pdbe.org/3hao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hao RCSB], [http://www.ebi.ac.uk/pdbsum/3hao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hao ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hao OCA], [https://pdbe.org/3hao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hao RCSB], [https://www.ebi.ac.uk/pdbsum/3hao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hao ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump.  
[[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump.  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ha/3hao_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ha/3hao_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 3hao" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3hao" 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: Bowie, J U]]
[[Category: Bowie, J U]]
[[Category: Joh, N H]]
[[Category: Joh, N H]]

Revision as of 14:57, 13 October 2021

Crystal structure of bacteriorhodopsin mutant L94A crystallized from bicellesCrystal structure of bacteriorhodopsin mutant L94A crystallized from bicelles

Structural highlights

3hao is a 2 chain structure with sequence from "bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:bop, VNG_1467G ("Bacillus halobius ruber" Klebahn 1919)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins.

Similar energetic contributions of packing in the core of membrane and water-soluble proteins.,Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU. Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 doi:10.1021/ja904711k

3hao, resolution 2.49Å

Drag the structure with the mouse to rotate

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OCA
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