3t1c: Difference between revisions

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<StructureSection load='3t1c' size='340' side='right'caption='[[3t1c]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3t1c' size='340' side='right'caption='[[3t1c]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3t1c]] 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=3T1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T1C FirstGlance]. <br>
<table><tr><td colspan='2'>[[3t1c]] 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=3T1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T1C 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></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]] 1.802&#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;'>[[3ouf|3ouf]], [[3t2m|3t2m]], [[3t4d|3t4d]]</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></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=226900 BACCR])</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=3t1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1c OCA], [https://pdbe.org/3t1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t1c RCSB], [https://www.ebi.ac.uk/pdbsum/3t1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1c 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=3t1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1c OCA], [https://pdbe.org/3t1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t1c RCSB], [https://www.ebi.ac.uk/pdbsum/3t1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1c 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]
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3t1c" 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: Baccr]]
[[Category: Bacillus cereus ATCC 14579]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Jiang, Y]]
[[Category: Jiang Y]]
[[Category: Raghunathan, S]]
[[Category: Raghunathan S]]
[[Category: Sauer, D B]]
[[Category: Sauer DB]]
[[Category: Zeng, W]]
[[Category: Zeng W]]
[[Category: Ion channel]]
[[Category: Membrane protein]]

Latest revision as of 12:58, 1 March 2024

Crystal Structure of NaK Channel D66Y MutantCrystal Structure of NaK Channel D66Y Mutant

Structural highlights

3t1c is a 2 chain structure with sequence from Bacillus cereus ATCC 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.802Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q81HW2_BACCR

See Also

3t1c, resolution 1.80Å

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