1f4z

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(New page: 200px<br /><applet load="1f4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4z, resolution 1.80&Aring;" /> '''BACTERIORHODOPSIN-M ...)
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[[Image:1f4z.jpg|left|200px]]<br /><applet load="1f4z" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1f4z, resolution 1.80&Aring;" />
 
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'''BACTERIORHODOPSIN-M PHOTOINTERMEDIATE STATE OF THE E204Q MUTANT AT 1.8 ANGSTROM RESOLUTION'''<br />
 
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==Overview==
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==BACTERIORHODOPSIN-M PHOTOINTERMEDIATE STATE OF THE E204Q MUTANT AT 1.8 ANGSTROM RESOLUTION==
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In order to understand how isomerization of the retinal drives, unidirectional transmembrane ion transport in bacteriorhodopsin, we, determined the atomic structures of the BR state and M photointermediate, of the E204Q mutant, to 1.7 and 1.8 A resolution, respectively. Comparison, of this M, in which proton release to the extracellular surface is, blocked, with the previously determined M in the D96N mutant indicates, that the changes in the extracellular region are initiated by changes in, the electrostatic interactions of the retinal Schiff base with Asp85 and, Asp212, but those on the cytoplasmic side originate from steric conflict, of the 13-methyl retinal group with Trp182 and distortion of the pi-bulge, of helix G. The structural changes suggest that protonation of Asp85, initiates a cascade of atomic displacements in the extracellular region, that cause release of a proton to the surface. The progressive relaxation, of the strained 13-cis retinal chain with deprotonated Schiff base, in, turn, initiates atomic displacements in the cytoplasmic region that cause, the intercalation of a hydrogen-bonded water molecule between Thr46 and, Asp96. This accounts for the lowering of the pK(a) of Asp96, which then, reprotonates the Schiff base via a newly formed chain of water molecules, that is extending toward the Schiff base.
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<StructureSection load='1f4z' size='340' side='right'caption='[[1f4z]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f4z]] is a 1 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=1F4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4Z 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]] 1.8&#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=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SQU:2,10,23-TRIMETHYL-TETRACOSANE'>SQU</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=1f4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4z OCA], [https://pdbe.org/1f4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4z RCSB], [https://www.ebi.ac.uk/pdbsum/1f4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4z 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/f4/1f4z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1f4z 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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In order to understand how isomerization of the retinal drives unidirectional transmembrane ion transport in bacteriorhodopsin, we determined the atomic structures of the BR state and M photointermediate of the E204Q mutant, to 1.7 and 1.8 A resolution, respectively. Comparison of this M, in which proton release to the extracellular surface is blocked, with the previously determined M in the D96N mutant indicates that the changes in the extracellular region are initiated by changes in the electrostatic interactions of the retinal Schiff base with Asp85 and Asp212, but those on the cytoplasmic side originate from steric conflict of the 13-methyl retinal group with Trp182 and distortion of the pi-bulge of helix G. The structural changes suggest that protonation of Asp85 initiates a cascade of atomic displacements in the extracellular region that cause release of a proton to the surface. The progressive relaxation of the strained 13-cis retinal chain with deprotonated Schiff base, in turn, initiates atomic displacements in the cytoplasmic region that cause the intercalation of a hydrogen-bonded water molecule between Thr46 and Asp96. This accounts for the lowering of the pK(a) of Asp96, which then reprotonates the Schiff base via a newly formed chain of water molecules that is extending toward the Schiff base.
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==About this Structure==
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Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin.,Luecke H, Schobert B, Cartailler JP, Richter HT, Rosengarth A, Needleman R, Lanyi JK J Mol Biol. 2000 Jul 28;300(5):1237-55. PMID:10903866<ref>PMID:10903866</ref>
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1F4Z 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F4Z 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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Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin., Luecke H, Schobert B, Cartailler JP, Richter HT, Rosengarth A, Needleman R, Lanyi JK, J Mol Biol. 2000 Jul 28;300(5):1237-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10903866 10903866]
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</div>
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[[Category: Halobacterium salinarum]]
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<div class="pdbe-citations 1f4z" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Cartailler, J.P.]]
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[[Category: Lanyi, J.K.]]
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[[Category: Luecke, H.]]
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[[Category: Needleman, R.]]
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[[Category: Richter, H.T.]]
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[[Category: Rosengarth, A.]]
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[[Category: Schobert, B.]]
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[[Category: LI1]]
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[[Category: RET]]
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[[Category: SQU]]
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[[Category: 7-transmembrane]]
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[[Category: e204q mutant m state]]
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[[Category: haloarchaea]]
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[[Category: ion pump]]
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[[Category: ion transport]]
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[[Category: lipids]]
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[[Category: membrane protein]]
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[[Category: merohedral twinning]]
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[[Category: photocycle intermediate]]
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[[Category: photoreceptor]]
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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 14:37:20 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: Cartailler JP]]
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[[Category: Lanyi JK]]
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[[Category: Luecke H]]
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[[Category: Needleman R]]
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[[Category: Richter HT]]
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[[Category: Rosengarth A]]
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[[Category: Schobert B]]

Current revision

BACTERIORHODOPSIN-M PHOTOINTERMEDIATE STATE OF THE E204Q MUTANT AT 1.8 ANGSTROM RESOLUTION

PDB ID 1f4z

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