6vx7

bestrophin-2 Ca2+-bound state (5 mM Ca2+)bestrophin-2 Ca2+-bound state (5 mM Ca2+)

Structural highlights 6vx7 is a 5 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Gene: BEST2 (BOVIN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [E1BF86_BOVIN] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126] Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6vx7, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image