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<StructureSection load='3k03' size='340' side='right'caption='[[3k03]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
<StructureSection load='3k03' size='340' side='right'caption='[[3k03]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3k03]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K03 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3k03]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K03 FirstGlance]. <br>
</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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k04|3k04]], [[3k06|3k06]], [[3k08|3k08]], [[3k0d|3k0d]], [[3k0g|3k0g]]</div></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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
<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=1396 ATCC 14579])</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=3k03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k03 OCA], [https://pdbe.org/3k03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k03 RCSB], [https://www.ebi.ac.uk/pdbsum/3k03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k03 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=3k03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k03 OCA], [https://pdbe.org/3k03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k03 RCSB], [https://www.ebi.ac.uk/pdbsum/3k03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k03 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q81HW2_BACCR Q81HW2_BACCR]
Selective ion conduction across ion channel pores is central to cellular physiology. To understand the underlying principles of ion selectivity in tetrameric cation channels, we engineered a set of cation channel pores based on the nonselective NaK channel and determined their structures to high resolution. These structures showcase an ensemble of selectivity filters with a various number of contiguous ion binding sites ranging from 2 to 4, with each individual site maintaining a geometry and ligand environment virtually identical to that of equivalent sites in K(+) channel selectivity filters. Combined with single channel electrophysiology, we show that only the channel with four ion binding sites is K(+) selective, whereas those with two or three are nonselective and permeate Na(+) and K(+) equally well. These observations strongly suggest that the number of contiguous ion binding sites in a single file is the key determinant of the channel's selectivity properties and the presence of four sites in K(+) channels is essential for highly selective and efficient permeation of K(+) ions.
 
Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites.,Derebe MG, Sauer DB, Zeng W, Alam A, Shi N, Jiang Y Proc Natl Acad Sci U S A. 2010 Dec 27. PMID:21187421<ref>PMID:21187421</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3k03" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 14579]]
[[Category: Bacillus cereus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Derebe, M G]]
[[Category: Derebe MG]]
[[Category: Jiang, Y]]
[[Category: Jiang Y]]
[[Category: Cng channel selectivity filter]]
[[Category: Cng mimicking]]
[[Category: Dtpp]]
[[Category: Ionic channel]]
[[Category: Nak]]
[[Category: Nak-dtpp]]
[[Category: Nak-mutant]]
[[Category: Transport protein]]

Latest revision as of 08:44, 7 February 2024

Crystal Structure of CNG mimicking NaK mutant, NaK-DTPP, K+ complex

3k03, resolution 1.62Å

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