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3t4d

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Current revision (10:02, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3t4d' size='340' side='right'caption='[[3t4d]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3t4d' size='340' side='right'caption='[[3t4d]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t4d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Baccr Baccr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T4D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t4d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T4D FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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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]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ouf|3ouf]], [[3t1c|3t1c]], [[3t2m|3t2m]]</div></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=K:POTASSIUM+ION'>K</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC_0669 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</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=3t4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t4d OCA], [https://pdbe.org/3t4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t4d RCSB], [https://www.ebi.ac.uk/pdbsum/3t4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t4d 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=3t4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t4d OCA], [https://pdbe.org/3t4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t4d RCSB], [https://www.ebi.ac.uk/pdbsum/3t4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t4d ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q81HW2_BACCR Q81HW2_BACCR]
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The structural and functional conversion of the nonselective NaK channel to a K(+) selective channel (NaK2K) allows us to identify two key residues, Tyr and Asp in the filter sequence of TVGYGD, that participate in interactions central to stabilizing the K(+) channel selectivity filter. By using protein crystallography and channel electrophysiology, we demonstrate that the K(+) channel filter exists as an energetically strained structure and requires these key protein interactions working in concert to hold the filter in the precisely defined four-sited configuration that is essential for selective K(+) permeation. Disruption of either interaction, as tested on both the NaK2K and eukaryotic K(v)1.6 channels, can reduce or completely abolish K(+) selectivity and in some cases may also lead to channel inactivation due to conformational changes at the filter. Additionally, on the scaffold of NaK we recapitulate the protein interactions found in the filter of the Kir channel family, which uses a distinct interaction network to achieve similar stabilization of the filter.
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Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation.,Sauer DB, Zeng W, Raghunathan S, Jiang Y Proc Natl Acad Sci U S A. 2011 Sep 20. PMID:21933962<ref>PMID:21933962</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t4d" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baccr]]
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[[Category: Bacillus cereus ATCC 14579]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jiang, Y]]
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[[Category: Jiang Y]]
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[[Category: Raghunathan, S]]
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[[Category: Raghunathan S]]
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[[Category: Sauer, D B]]
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[[Category: Sauer DB]]
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[[Category: Zeng, W]]
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[[Category: Zeng W]]
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[[Category: Ion channel]]
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[[Category: Membrane protein]]
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Current revision

Crystal Structure of NaK2K Channel Y55F Mutant

PDB ID 3t4d

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