3tet

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:08, 1 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3tet' size='340' side='right'caption='[[3tet]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3tet' size='340' side='right'caption='[[3tet]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3tet]] 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=3TET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TET FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3tet]] 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=3TET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TET 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]] 1.9&#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]], [[3t4d|3t4d]], [[3t4z|3t4z]]</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=3tet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tet OCA], [https://pdbe.org/3tet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tet RCSB], [https://www.ebi.ac.uk/pdbsum/3tet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tet 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=3tet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tet OCA], [https://pdbe.org/3tet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tet RCSB], [https://www.ebi.ac.uk/pdbsum/3tet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tet 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 3tet" 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]]
+

Current revision

Crystal Structure of NaK2K Channel Y66F Mutant

PDB ID 3tet

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3tet"
Personal tools