1s5h
From Proteopedia
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- | [[Image:1s5h.png|left|200px]] | ||
- | < | + | ==Potassium Channel Kcsa-Fab Complex T75C mutant in K+== |
- | + | <StructureSection load='1s5h' size='340' side='right'caption='[[1s5h]], [[Resolution|resolution]] 2.20Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1s5h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus], [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] 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=1S5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S5H FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=K:POTASSIUM+ION'>K</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=1s5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5h OCA], [https://pdbe.org/1s5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s5h RCSB], [https://www.ebi.ac.uk/pdbsum/1s5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s5h ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/KCSA_STRCO KCSA_STRCO] Acts as a potassium ion channel (By similarity). | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s5/1s5h_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s5h ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The selectivity filter of K(+) channels is comprised of a linear queue of four equal-spaced ion-binding sites spanning a distance of 12A. Each site is formed of eight oxygen atoms from the protein. The first three sites, numbered 1-3 from the extracellular side, are made of exclusively main-chain carbonyl oxygen atoms. The fourth site, closest to the intracellular side, is made of four main-chain carbonyl oxygen atoms and four threonine side-chain hydroxyl oxygen atoms. Here we characterize the effects of mutating the threonine to cysteine on the distribution of ions in the selectivity filter and on the conduction of ions through the filter. The mutation influences the occupancy of K(+) at sites 2 and 4 and it reduces the maximum rate of conduction in the limit of high K(+) concentration. The mutation does not affect the conduction of Rb(+). These results can be understood in the context of a conduction mechanism in which a pair of K ions switch between energetically balanced 1,3 and 2,4 configurations. | ||
- | + | A mutant KcsA K(+) channel with altered conduction properties and selectivity filter ion distribution.,Zhou M, MacKinnon R J Mol Biol. 2004 May 7;338(4):839-46. PMID:15099749<ref>PMID:15099749</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1s5h" style="background-color:#fffaf0;"></div> | |
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- | == | + | |
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==See Also== | ==See Also== | ||
- | *[[ | + | *[[Antibody 3D structures|Antibody 3D structures]] |
- | *[[Potassium | + | *[[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: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
- | [[Category: Streptomyces coelicolor | + | [[Category: Streptomyces coelicolor]] |
- | [[Category: | + | [[Category: Streptomyces lividans]] |
- | [[Category: | + | [[Category: Mackinnon R]] |
- | [[Category: | + | [[Category: Zhou M]] |
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Current revision
Potassium Channel Kcsa-Fab Complex T75C mutant in K+
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