5vke

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Open conformation of KcsA deep-inactivated

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 <StructureSection load='5vke' size='340' side='right'caption='[[5vke]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5vke]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965] 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=5VKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VKE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5vke]] 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=5VKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VKE 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vk6|5vk6]], [[5vkh|5vkh]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 "Actinomyces lividans" Krasil'nikov et al. 1965])</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=5vke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vke OCA], [https://pdbe.org/5vke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vke RCSB], [https://www.ebi.ac.uk/pdbsum/5vke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vke ProSAT]</span></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=5vke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vke OCA], [http://pdbe.org/5vke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vke RCSB], [http://www.ebi.ac.uk/pdbsum/5vke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vke 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>
+[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 ==
-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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5vke" 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/>
 __TOC__
 </StructureSection>
-[[Category: Actinomyces lividans krasil'nikov et al. 1965]]
 [[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Cortes, D M]]
+[[Category: Streptomyces lividans]]
-[[Category: Cuello, L G]]
+[[Category: Cortes DM]]
-[[Category: Perozo, E]]
+[[Category: Cuello LG]]
-[[Category: Deep-inactivated]]
+[[Category: Perozo E]]
-[[Category: Immune system-transport protein complex]]
-[[Category: Kcsa]]
-[[Category: Open]]
-[[Category: Potassium channel]]

5vke

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Open conformation of KcsA deep-inactivated

Structural highlights

Function

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