1s5h: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='1s5h' size='340' side='right'caption='[[1s5h]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1s5h' size='340' side='right'caption='[[1s5h]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1s5h]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1s5h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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='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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KCSA, SKC1, SCO7660, SC10F4.33 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KCSA, SKC1, SCO7660, SC10F4.33 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 "Actinomyces coelicolor" (Muller 1908) Lieske 1921])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/KCSA_STRCO KCSA_STRCO]] Acts as a potassium ion channel (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:30, 27 October 2021
Potassium Channel Kcsa-Fab Complex T75C mutant in K+Potassium Channel Kcsa-Fab Complex T75C mutant in K+
Structural highlights
Function[KCSA_STRCO] Acts as a potassium ion channel (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||