5vkh: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5vkh is ~~ON HOLD~~ ~~until Paper~~ Publication

==Closed conformation of KcsA Y82A-F103A mutant==

== Structural highlights ==

<table><tr><td colspan='2'>[[5vkh]] 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=5VKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VKH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1EM:(1S)-2-HYDROXY-1-[(NONANOYLOXY)METHYL]ETHYL+MYRISTATE'>1EM</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vk6|5vk6]], [[5vke|5vke]]</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=5vkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vkh OCA], [http://pdbe.org/5vkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vkh RCSB], [http://www.ebi.ac.uk/pdbsum/5vkh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vkh ProSAT]</span></td></tr>

</table>

== 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>

== Publication Abstract from PubMed ==

C-type inactivation in potassium channels helps fine-tune long-term channel activity through conformational changes at the selectivity filter. Here, through the use of cross-linked constitutively open constructs, we determined the structures of KcsA's mutants that stabilize the selectivity filter in its conductive (E71A, at 2.25 A) and deep C-type inactivated (Y82A at 2.4 A) conformations. These structural snapshots represent KcsA's transient open-conductive (O/O) and the stable open deep C-type inactivated states (O/I), respectively. The present structures provide an unprecedented view of the selectivity filter backbone in its collapsed deep C-type inactivated conformation, highlighting the close interactions with structural waters and the local allosteric interactions that couple activation and inactivation gating. Together with the structures associated with the closed-inactivated state (C/I) and in the well-known closed conductive state (C/O), this work recapitulates, at atomic resolution, the key conformational changes of a potassium channel pore domain as it progresses along its gating cycle.

~~Authors:~~ Cuello, ~~L.G.~~, Perozo, E.~~, Cortes, D~~.M.

The gating cycle of a K(+) channel at atomic resolution.,Cuello LG, Cortes DM, Perozo E Elife. 2017 Nov 22;6. doi: 10.7554/eLife.28032. PMID:29165243<ref>PMID:29165243</ref>

~~Description: Closed conformation~~ of ~~KcsA Y82A~~-~~F103A mutant~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

[[Category: Cuello, L.G]]

== References ==

__TOC__

</StructureSection>

[[Category: Mus musculus]]

[[Category: Cortes, D M]]

[[Category: Cuello, L G]]

[[Category: Perozo, E]]

[[Category: ~~Cortes, D.M~~]]

[[Category: Closed]]

[[Category: Immune system-transport protein complex]]

[[Category: Kcsa]]

[[Category: Potassium channel]]

[[Category: Y82a-f103a]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5vkh is ON HOLD  until Paper Publication
+==Closed conformation of KcsA Y82A-F103A mutant==
+<StructureSection load='5vkh' size='340' side='right' caption='[[5vkh]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5vkh]] 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=5VKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VKH FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1EM:(1S)-2-HYDROXY-1-[(NONANOYLOXY)METHYL]ETHYL+MYRISTATE'>1EM</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vk6|5vk6]], [[5vke|5vke]]</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=5vkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vkh OCA], [http://pdbe.org/5vkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vkh RCSB], [http://www.ebi.ac.uk/pdbsum/5vkh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vkh ProSAT]</span></td></tr>
+</table>
+== 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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+C-type inactivation in potassium channels helps fine-tune long-term channel activity through conformational changes at the selectivity filter. Here, through the use of cross-linked constitutively open constructs, we determined the structures of KcsA's mutants that stabilize the selectivity filter in its conductive (E71A, at 2.25 A) and deep C-type inactivated (Y82A at 2.4 A) conformations. These structural snapshots represent KcsA's transient open-conductive (O/O) and the stable open deep C-type inactivated states (O/I), respectively. The present structures provide an unprecedented view of the selectivity filter backbone in its collapsed deep C-type inactivated conformation, highlighting the close interactions with structural waters and the local allosteric interactions that couple activation and inactivation gating. Together with the structures associated with the closed-inactivated state (C/I) and in the well-known closed conductive state (C/O), this work recapitulates, at atomic resolution, the key conformational changes of a potassium channel pore domain as it progresses along its gating cycle.
-Authors: Cuello, L.G., Perozo, E., Cortes, D.M.
+The gating cycle of a K(+) channel at atomic resolution.,Cuello LG, Cortes DM, Perozo E Elife. 2017 Nov 22;6. doi: 10.7554/eLife.28032. PMID:29165243<ref>PMID:29165243</ref>
-Description: Closed conformation of KcsA Y82A-F103A mutant
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Cuello, L.G]]
+<div class="pdbe-citations 5vkh" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Mus musculus]]
+[[Category: Cortes, D M]]
+[[Category: Cuello, L G]]
 [[Category: Perozo, E]]
-[[Category: Cortes, D.M]]
+[[Category: Closed]]
+[[Category: Immune system-transport protein complex]]
+[[Category: Kcsa]]
+[[Category: Potassium channel]]
+[[Category: Y82a-f103a]]