6vx9: Difference between revisions
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<StructureSection load='6vx9' size='340' side='right'caption='[[6vx9]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='6vx9' size='340' side='right'caption='[[6vx9]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6vx9]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VX9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VX9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6vx9]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VX9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VX9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BEST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vx9 OCA], [http://pdbe.org/6vx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vx9 RCSB], [http://www.ebi.ac.uk/pdbsum/6vx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vx9 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vx9 OCA], [http://pdbe.org/6vx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vx9 RCSB], [http://www.ebi.ac.uk/pdbsum/6vx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vx9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/E1BF86_BOVIN E1BF86_BOVIN]] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126] | [[http://www.uniprot.org/uniprot/E1BF86_BOVIN E1BF86_BOVIN]] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bestrophin family of calcium (Ca(2+))-activated chloride (Cl(-)) channels, which mediate the influx and efflux of monovalent anions in response to the levels of intracellular Ca(2+), comprises four members in mammals (bestrophin 1-4). Here we report cryo-EM structures of bovine bestrophin-2 (bBest2) bound and unbound by Ca(2+) at 2.4- and 2.2-A resolution, respectively. The bBest2 structure highlights four previously underappreciated pore-lining residues specifically conserved in Best2 but not in Best1, illustrating the differences between these paralogs. Structure-inspired electrophysiological analysis reveals that, although the channel is sensitive to Ca(2+), it has substantial Ca(2+)-independent activity for Cl(-), reflecting the opening at the cytoplasmic restriction of the ion conducting pathway even when Ca(2+) is absent. Moreover, the ion selectivity of bBest2 is controlled by multiple residues, including those involved in gating. | |||
Structural and functional characterization of the bestrophin-2 anion channel.,Owji AP, Zhao Q, Ji C, Kittredge A, Hopiavuori A, Fu Z, Ward N, Clarke OB, Shen Y, Zhang Y, Hendrickson WA, Yang T Nat Struct Mol Biol. 2020 Apr;27(4):382-391. doi: 10.1038/s41594-020-0402-z. Epub, 2020 Apr 6. PMID:32251414<ref>PMID:32251414</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6vx9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bovin]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Clarke, O]] | [[Category: Clarke, O]] | ||
Revision as of 09:13, 22 April 2020
bestrophin-2 Ca2+- unbound state 1 (EGTA only)bestrophin-2 Ca2+- unbound state 1 (EGTA only)
Structural highlights
Function[E1BF86_BOVIN] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126] Publication Abstract from PubMedThe bestrophin family of calcium (Ca(2+))-activated chloride (Cl(-)) channels, which mediate the influx and efflux of monovalent anions in response to the levels of intracellular Ca(2+), comprises four members in mammals (bestrophin 1-4). Here we report cryo-EM structures of bovine bestrophin-2 (bBest2) bound and unbound by Ca(2+) at 2.4- and 2.2-A resolution, respectively. The bBest2 structure highlights four previously underappreciated pore-lining residues specifically conserved in Best2 but not in Best1, illustrating the differences between these paralogs. Structure-inspired electrophysiological analysis reveals that, although the channel is sensitive to Ca(2+), it has substantial Ca(2+)-independent activity for Cl(-), reflecting the opening at the cytoplasmic restriction of the ion conducting pathway even when Ca(2+) is absent. Moreover, the ion selectivity of bBest2 is controlled by multiple residues, including those involved in gating. Structural and functional characterization of the bestrophin-2 anion channel.,Owji AP, Zhao Q, Ji C, Kittredge A, Hopiavuori A, Fu Z, Ward N, Clarke OB, Shen Y, Zhang Y, Hendrickson WA, Yang T Nat Struct Mol Biol. 2020 Apr;27(4):382-391. doi: 10.1038/s41594-020-0402-z. Epub, 2020 Apr 6. PMID:32251414[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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