1zwi

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(New page: 200px<br /> <applet load="1zwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zwi, resolution 2.50&Aring;" /> '''Structure of mutant...)
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[[Image:1zwi.gif|left|200px]]<br />
 
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<applet load="1zwi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zwi, resolution 2.50&Aring;" />
 
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'''Structure of mutant KcsA potassium channel'''<br />
 
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==Overview==
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==Structure of mutant KcsA potassium channel==
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We show that in the potassium channel KcsA, proton-dependent activation is, followed by an inactivation process similar to C-type inactivation, and, this process is suppressed by an E71A mutation in the pore helix. EPR, spectroscopy demonstrates that the inner gate opens maximally at low pH, regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at, the selectivity filter. Two E71A crystal structures obtained at 2.5 A, reveal large structural excursions of the selectivity filter during ion, conduction and provide a glimpse of the range of conformations available, to this region of the channel during gating. These data establish a, mechanistic basis for the role of the selectivity filter during channel, activation and inactivation.
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<StructureSection load='1zwi' size='340' side='right'caption='[[1zwi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zwi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZWI 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]] 2.5&#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=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=1zwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zwi OCA], [https://pdbe.org/1zwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zwi RCSB], [https://www.ebi.ac.uk/pdbsum/1zwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zwi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KCSA_STRLI KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).<ref>PMID:7489706</ref>
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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/zw/1zwi_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=1zwi 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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We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.
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==About this Structure==
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Molecular determinants of gating at the potassium-channel selectivity filter.,Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, Roux B, Perozo E Nat Struct Mol Biol. 2006 Apr;13(4):311-8. Epub 2006 Mar 12. PMID:16532009<ref>PMID:16532009</ref>
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1ZWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans] with K, DGA and F09 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZWI 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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Molecular determinants of gating at the potassium-channel selectivity filter., Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, Roux B, Perozo E, Nat Struct Mol Biol. 2006 Apr;13(4):311-8. Epub 2006 Mar 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16532009 16532009]
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</div>
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<div class="pdbe-citations 1zwi" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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*[[Potassium channel 3D structures|Potassium channel 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: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
 
[[Category: Streptomyces lividans]]
[[Category: Streptomyces lividans]]
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[[Category: Cordero-Morales, J.F.]]
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[[Category: Cordero-Morales JF]]
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[[Category: Cortes, D.M.]]
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[[Category: Cortes DM]]
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[[Category: Cuello, L.G.]]
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[[Category: Cuello LG]]
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[[Category: Jogini, V.]]
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[[Category: Jogini V]]
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[[Category: Perozo, E.]]
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[[Category: Perozo E]]
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[[Category: Roux, B.]]
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[[Category: Roux B]]
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[[Category: Zhao, Y.]]
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[[Category: Zhao Y]]
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[[Category: DGA]]
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[[Category: F09]]
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[[Category: K]]
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[[Category: x-ray crystallography; potassium ion channel; transmembrane protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:46:20 2007''
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Current revision

Structure of mutant KcsA potassium channel

PDB ID 1zwi

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