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| | <StructureSection load='3gb7' size='340' side='right'caption='[[3gb7]], [[Resolution|resolution]] 2.85Å' scene=''> | | <StructureSection load='3gb7' size='340' side='right'caption='[[3gb7]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gb7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965] 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=3GB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GB7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gb7]] 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=3GB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GB7 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=NI:NICKEL+(II)+ION'>NI</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]] 2.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kcsA, skc1 ([https://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='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=NI:NICKEL+(II)+ION'>NI</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=3gb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gb7 OCA], [https://pdbe.org/3gb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gb7 RCSB], [https://www.ebi.ac.uk/pdbsum/3gb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gb7 ProSAT]</span></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=3gb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gb7 OCA], [https://pdbe.org/3gb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gb7 RCSB], [https://www.ebi.ac.uk/pdbsum/3gb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gb7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces lividans krasil'nikov et al. 1965]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Allen, T W]] | + | [[Category: Streptomyces lividans]] |
| - | [[Category: Ilsoo, K]] | + | [[Category: Allen TW]] |
| - | [[Category: Iverson, T M]] | + | [[Category: Ilsoo K]] |
| - | [[Category: Nimigean, C M]] | + | [[Category: Iverson TM]] |
| - | [[Category: Panosian, T D]] | + | [[Category: Nimigean CM]] |
| - | [[Category: Thompson, A N]] | + | [[Category: Panosian TD]] |
| - | [[Category: Cell membrane]]
| + | [[Category: Thompson AN]] |
| - | [[Category: Integral membrane protein]]
| + | |
| - | [[Category: Ion selectivity]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Ion-channel]]
| + | |
| - | [[Category: Ionic channel]]
| + | |
| - | [[Category: Lithium block]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Potassium transport]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Voltage-gated channel]]
| + | |
| - | [[Category: Voltage-gated potassium channel]]
| + | |
| Structural highlights
Function
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(+).[1]
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 PubMed
Potassium channels allow K(+) ions to diffuse through their pores while preventing smaller Na(+) ions from permeating. Discrimination between these similar, abundant ions enables these proteins to control electrical and chemical activity in all organisms. Selection occurs at the narrow selectivity filter containing structurally identified K(+) binding sites. Selectivity is thought to arise because smaller ions such as Na(+) do not bind to these K(+) sites in a thermodynamically favorable way. Using the model K(+) channel KcsA, we examined how intracellular Na(+) and Li(+) interact with the pore and the permeant ions using electrophysiology, molecular dynamics simulations and X-ray crystallography. Our results suggest that these small cations have a separate binding site within the K(+) selectivity filter. We propose that selective permeation from the intracellular side primarily results from a large energy barrier blocking filter entry for Na(+) and Li(+) in the presence of K(+), not from a difference of binding affinity between ions.
Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore.,Thompson AN, Kim I, Panosian TD, Iverson TM, Allen TW, Nimigean CM Nat Struct Mol Biol. 2009 Dec;16(12):1317-24. Epub 2009 Nov 29. PMID:19946269[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 1995 Nov 1;14(21):5170-8. PMID:7489706
- ↑ Thompson AN, Kim I, Panosian TD, Iverson TM, Allen TW, Nimigean CM. Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore. Nat Struct Mol Biol. 2009 Dec;16(12):1317-24. Epub 2009 Nov 29. PMID:19946269 doi:10.1038/nsmb.1703
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