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4wd8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae== | |
| + | <StructureSection load='4wd8' size='340' side='right'caption='[[4wd8]], [[Resolution|resolution]] 2.30Å' 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]] 2.3Å</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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <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]] | ||
Current revision
Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae
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