1tn5

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(New page: 200px<br /><applet load="1tn5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tn5, resolution 2.2&Aring;" /> '''Structure of bacteror...)
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[[Image:1tn5.jpg|left|200px]]<br /><applet load="1tn5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tn5, resolution 2.2&Aring;" />
 
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'''Structure of bacterorhodopsin mutant K41P'''<br />
 
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==Overview==
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==Structure of bacterorhodopsin mutant K41P==
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Proline residues are relatively common in transmembrane helices. This, suggests that proline substitutions may be readily tolerated in membrane, proteins, even though they invariably produce deviations from canonical, helical structure. We have experimentally tested this possibility by, making proline substitutions at 15 positions throughout the N-terminal, half of bacteriorhodopsin helix B. We find that six of the substitutions, yielded no active protein and all the others were destabilizing. Three, mutations were only slightly destabilizing, however, reducing stability by, about 0.5 kcal/mol, and these all occurred close to the N terminus. This, result is consistent with the observation that proline is more common near, the ends of TM helices. To learn how proline side-chains could be, structurally accommodated at different locations in the helix, we solved, the structures of a moderately destabilized mutant positioned near the N, terminus of the helix, K41P, and a severely destabilized mutant positioned, near the middle of the helix, A51P. The K41P mutation produced only local, structural alterations, while the A51P mutation resulted in small, but, widely distributed structural changes in helix B. Our results indicate, that proline is not easily accommodated in transmembrane helices and that, the tolerance to proline substitution is dependent, in a complex way, on, the position in the structure.
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<StructureSection load='1tn5' size='340' side='right'caption='[[1tn5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tn5]] is a 2 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=1TN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TN5 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]] 2.2&#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=RET:RETINAL'>RET</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=1tn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tn5 OCA], [https://pdbe.org/1tn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tn5 RCSB], [https://www.ebi.ac.uk/pdbsum/1tn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tn5 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/tn/1tn5_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=1tn5 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TN5 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 RET as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TN5 OCA].
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*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Proline substitutions are not easily accommodated in a membrane protein., Yohannan S, Yang D, Faham S, Boulting G, Whitelegge J, Bowie JU, J Mol Biol. 2004 Jul 30;341(1):1-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15312757 15312757]
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[[Category: Halobacterium salinarum]]
[[Category: Halobacterium salinarum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Boulting, G.]]
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[[Category: Boulting G]]
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[[Category: Bowie, J.U.]]
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[[Category: Bowie JU]]
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[[Category: Faham, S.]]
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[[Category: Faham S]]
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[[Category: Whitelegge, J.]]
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[[Category: Whitelegge J]]
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[[Category: Yang, D.]]
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[[Category: Yang D]]
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[[Category: Yohannan, S.]]
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[[Category: Yohannan S]]
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[[Category: RET]]
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[[Category: bacteriorhodopsin]]
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[[Category: bicelle]]
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[[Category: membrane protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:25:32 2007''
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Current revision

Structure of bacterorhodopsin mutant K41P

PDB ID 1tn5

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