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5vkh
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Closed conformation of KcsA Y82A-F103A mutant== | |
| + | <StructureSection load='5vkh' size='340' side='right' caption='[[5vkh]], [[Resolution|resolution]] 2.25Å' 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cuello, L | + | <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: Perozo, E]] | ||
| - | [[Category: | + | [[Category: Closed]] |
| + | [[Category: Immune system-transport protein complex]] | ||
| + | [[Category: Kcsa]] | ||
| + | [[Category: Potassium channel]] | ||
| + | [[Category: Y82a-f103a]] | ||
Revision as of 07:15, 6 December 2017
Closed conformation of KcsA Y82A-F103A mutant
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