1brr

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(New page: 200px<br /><applet load="1brr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1brr, resolution 2.9&Aring;" /> '''X-RAY STRUCTURE OF TH...)
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[[Image:1brr.gif|left|200px]]<br /><applet load="1brr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1brr, resolution 2.9&Aring;" />
 
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'''X-RAY STRUCTURE OF THE BACTERIORHODOPSIN TRIMER/LIPID COMPLEX'''<br />
 
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==Overview==
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==X-RAY STRUCTURE OF THE BACTERIORHODOPSIN TRIMER/LIPID COMPLEX==
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Heterogenous nucleation on small molecule crystals causes a monoclinic, crystal form of bacteriorhodopsin (BR) in which trimers of this membrane, protein pack differently than in native purple membranes. Analysis of, single crystals by nano-electrospray ionization-mass spectrometry, demonstrated a preservation of the purple membrane lipid composition in, these BR crystals. The 2.9-A x-ray structure shows a lipid-mediated, stabilization of BR trimers where the glycolipid S-TGA-1 binds into the, central compartment of BR trimers. The BR trimer/lipid complex provides an, example of local membrane thinning as the lipid head-group boundary of the, central lipid patch is shifted by 5 A toward the membrane center., Nonbiased electron density maps reveal structural differences to, previously reported BR structures, especially for the cytosolic EF loop, and the proton exit pathway. The terminal proton release complex now, comprises an E194-E204 dyad as a diffuse proton buffer.
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<StructureSection load='1brr' size='340' side='right'caption='[[1brr]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1brr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARC:3,7,11,15-TETRAMETHYL-HEXADECAN-1-OL'>ARC</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SGA:O3-SULFONYLGALACTOSE'>SGA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1brr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brr OCA], [https://pdbe.org/1brr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1brr RCSB], [https://www.ebi.ac.uk/pdbsum/1brr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1brr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1brr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Heterogenous nucleation on small molecule crystals causes a monoclinic crystal form of bacteriorhodopsin (BR) in which trimers of this membrane protein pack differently than in native purple membranes. Analysis of single crystals by nano-electrospray ionization-mass spectrometry demonstrated a preservation of the purple membrane lipid composition in these BR crystals. The 2.9-A x-ray structure shows a lipid-mediated stabilization of BR trimers where the glycolipid S-TGA-1 binds into the central compartment of BR trimers. The BR trimer/lipid complex provides an example of local membrane thinning as the lipid head-group boundary of the central lipid patch is shifted by 5 A toward the membrane center. Nonbiased electron density maps reveal structural differences to previously reported BR structures, especially for the cytosolic EF loop and the proton exit pathway. The terminal proton release complex now comprises an E194-E204 dyad as a diffuse proton buffer.
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==About this Structure==
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Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex.,Essen L, Siegert R, Lehmann WD, Oesterhelt D Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11673-8. PMID:9751724<ref>PMID:9751724</ref>
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1BRR 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 GLC, RET, ARC, OCT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BRR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex , Essen L, Siegert R, Lehmann WD, Oesterhelt D, Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11673-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9751724 9751724]
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</div>
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[[Category: Halobacterium salinarum]]
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<div class="pdbe-citations 1brr" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Essen, L.O.]]
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[[Category: Oesterhelt, D.]]
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[[Category: Siegert, R.]]
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[[Category: ARC]]
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[[Category: GLC]]
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[[Category: GOL]]
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[[Category: OCT]]
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[[Category: RET]]
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[[Category: haloarchaea]]
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[[Category: lipids]]
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[[Category: membrane protein]]
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[[Category: photoreceptor]]
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[[Category: proton pump]]
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[[Category: retinal protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:51:55 2007''
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==See Also==
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*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Halobacterium salinarum]]
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[[Category: Large Structures]]
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[[Category: Essen L-O]]
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[[Category: Oesterhelt D]]
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[[Category: Siegert R]]

Current revision

X-RAY STRUCTURE OF THE BACTERIORHODOPSIN TRIMER/LIPID COMPLEX

PDB ID 1brr

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