4wd7

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'''Unreleased structure'''
 
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The entry 4wd7 is ON HOLD
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==Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae by Zn-SAD phasing==
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<StructureSection load='4wd7' size='340' side='right'caption='[[4wd7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4wd7]] 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=4WD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WD7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=ZN:ZINC+ION'>ZN</scene></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=4wd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wd7 OCA], [https://pdbe.org/4wd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wd7 RCSB], [https://www.ebi.ac.uk/pdbsum/4wd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wd7 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Yang, T., Liu, Q., Hendrickson, W.A., New York Consortium on Membrane Protein Structure (NYCOMPS)
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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>
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Description:
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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 4wd7" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Bestrophin 3D structures|Bestrophin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Klebsiella pneumoniae UHKPC96]]
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[[Category: Large Structures]]
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[[Category: Hendrickson WA]]
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[[Category: Liu Q]]
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[[Category: Yang T]]

Current revision

Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae by Zn-SAD phasing

PDB ID 4wd7

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