6pa0: Difference between revisions

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<StructureSection load='6pa0' size='340' side='right'caption='[[6pa0]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='6pa0' size='340' side='right'caption='[[6pa0]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6pa0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PA0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6pa0]] 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=6PA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PA0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.05&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pa0 OCA], [http://pdbe.org/6pa0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pa0 RCSB], [http://www.ebi.ac.uk/pdbsum/6pa0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pa0 ProSAT]</span></td></tr>
<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=NA:SODIUM+ION'>NA</scene></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=6pa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pa0 OCA], [https://pdbe.org/6pa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pa0 RCSB], [https://www.ebi.ac.uk/pdbsum/6pa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pa0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Here, we present the atomic resolution crystallographic structure, the function, and the ion-binding properties of the KcsA mutants, G77A and G77C, that stabilize the 2,4-ion-bound configuration (i.e., water, K(+), water, K(+)-ion-bound configuration) of the K(+) channel's selectivity filter. A full functional and thermodynamic characterization of the G77A mutant revealed wild-type-like ion selectivity and apparent K(+)-binding affinity, in addition to showing a lack of C-type inactivation gating and a marked reduction in its single-channel conductance. These structures validate, from a structural point of view, the notion that 2 isoenergetic ion-bound configurations coexist within a K(+) channel's selectivity filter, which fully agrees with the water-K(+)-ion-coupled transport detected by streaming potential measurements.
 
Structure, function, and ion-binding properties of a K(+) channel stabilized in the 2,4-ion-bound configuration.,Tilegenova C, Cortes DM, Jahovic N, Hardy E, Hariharan P, Guan L, Cuello LG Proc Natl Acad Sci U S A. 2019 Aug 6. pii: 1901888116. doi:, 10.1073/pnas.1901888116. PMID:31387976<ref>PMID:31387976</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pa0" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Cuello, L G]]
[[Category: Streptomyces lividans]]
[[Category: Guan, L]]
[[Category: Cuello LG]]
[[Category: Kcsa]]
[[Category: Guan L]]
[[Category: Permeation]]
[[Category: Potassium channel]]
[[Category: Protein transport]]
[[Category: Protein transport-immune system complex]]
[[Category: Selectivity]]
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