View source for 6n25


==BEST1 open state W287F mutant, calcium-bound==
<SX load='6n25' size='340' side='right' viewer='molstar' caption='[[6n25]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6n25]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N25 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=6n25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n25 OCA], [https://pdbe.org/6n25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n25 RCSB], [https://www.ebi.ac.uk/pdbsum/6n25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n25 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Bestrophin (BEST1-4) ligand-gated chloride (Cl(-)) channels are activated by calcium (Ca(2+)). Mutation of BEST1 causes retinal disease. Partly because bestrophin channels have no sequence or structural similarity to other ion channels, the molecular mechanisms underlying gating are unknown. Here, we present a series of cryo-electron microscopy structures of chicken BEST1, determined at 3.1 A resolution or better, that represent the channel's principal gating states. Unlike other channels, opening of the pore is due to the repositioning of tethered pore-lining helices within a surrounding protein shell that dramatically widens a neck of the pore through a concertina of amino acid rearrangements. The neck serves as both the activation and the inactivation gate. Ca(2+) binding instigates opening of the neck through allosteric means whereas inactivation peptide binding induces closing. An aperture within the otherwise wide pore controls anion permeability. The studies define a new molecular paradigm for gating among ligand-gated ion channels.

Molecular mechanisms of gating in the calcium-activated chloride channel bestrophin.,Miller AN, Vaisey G, Long SB Elife. 2019 Jan 10;8. pii: 43231. doi: 10.7554/eLife.43231. PMID:30628889<ref>PMID:30628889</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6n25" style="background-color:#fffaf0;"></div>

==See Also==
*[[Bestrophin 3D structures|Bestrophin 3D structures]]
== References ==
<references/>
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[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Long SB]]
[[Category: Miller AN]]
[[Category: Vaisey G]]