View source for 4wd8


==Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae==
<StructureSection load='4wd8' size='340' side='right'caption='[[4wd8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wd8]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_UHKPC96 Klebsiella pneumoniae UHKPC96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WD8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4wd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wd8 OCA], [https://pdbe.org/4wd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wd8 RCSB], [https://www.ebi.ac.uk/pdbsum/4wd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wd8 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Human bestrophin-1 (hBest1) is a calcium-activated chloride channel from the retinal pigment epithelium, where mutations are associated with vitelliform macular degeneration, or Best disease. We describe the structure of a bacterial homolog (KpBest) of hBest1 and functional characterizations of both channels. KpBest is a pentamer that forms a five-helix transmembrane pore, closed by three rings of conserved hydrophobic residues, and has a cytoplasmic cavern with a restricted exit. From electrophysiological analysis of structure-inspired mutations in KpBest and hBest1, we find a sensitive control of ion selectivity in the bestrophins, including reversal of anion/cation selectivity, and dramatic activation by mutations at the cytoplasmic exit. A homology model of hBest1 shows the locations of disease-causing mutations and suggests possible roles in regulation.

Structure and selectivity in bestrophin ion channels.,Yang T, Liu Q, Kloss B, Bruni R, Kalathur RC, Guo Y, Kloppmann E, Rost B, Colecraft HM, Hendrickson WA Science. 2014 Oct 17;346(6207):355-9. doi: 10.1126/science.1259723. Epub 2014 Sep, 25. PMID:25324390<ref>PMID:25324390</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 4wd8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Bestrophin 3D structures|Bestrophin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae UHKPC96]]
[[Category: Large Structures]]
[[Category: Hendrickson WA]]
[[Category: Liu Q]]
[[Category: Yang T]]