6vx9

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Current revision (14:40, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6vx9' size='340' side='right'caption='[[6vx9]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
<StructureSection load='6vx9' size='340' side='right'caption='[[6vx9]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[6vx9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6VX9 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
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<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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vx9 OCA], [https://pdbe.org/6vx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vx9 RCSB], [https://www.ebi.ac.uk/pdbsum/6vx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vx9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/E1BF86_BOVIN E1BF86_BOVIN]] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126]
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[https://www.uniprot.org/uniprot/E1BF86_BOVIN E1BF86_BOVIN] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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==See Also==
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*[[Bestrophin 3D structures|Bestrophin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6vx9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bovin]]
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[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Clarke, O]]
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[[Category: Clarke O]]
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[[Category: Fu, Z]]
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[[Category: Fu Z]]
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[[Category: Hendrickson, W A]]
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[[Category: Hendrickson WA]]
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[[Category: Hopiavuori, A]]
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[[Category: Hopiavuori A]]
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[[Category: Ji, C]]
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[[Category: Ji C]]
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[[Category: Kittredge, A]]
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[[Category: Kittredge A]]
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[[Category: Owji, A P]]
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[[Category: Owji AP]]
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[[Category: Shen, Y]]
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[[Category: Shen Y]]
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[[Category: Ward, N]]
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[[Category: Ward N]]
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[[Category: Yang, T]]
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[[Category: Yang T]]
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[[Category: Zhang, Y]]
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[[Category: Zhang Y]]
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[[Category: Zhao, Q]]
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[[Category: Zhao Q]]
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[[Category: Chloride channel]]
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[[Category: Membrane protein]]
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Current revision

bestrophin-2 Ca2+- unbound state 1 (EGTA only)

PDB ID 6vx9

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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