8ecy | pdb_00008ecy

cryoEM structure of bovine bestrophin-2 and glutamine synthetase complex

spinqualitylabelsall models 8ecy, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ecy is a 15 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2Å Ligands: CA, CL, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BEST2_BOVIN Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (PubMed:32251414, PubMed:36289327). Transports a large specter of anions, namely mediates the movement of chloride, L-glutamate and iodide (PubMed:32251414, PubMed:36289327). Calcium-binding triggers the dilation of the aperture, but calcium-dependent gating is only effective when the size of the passing anion is bigger than the closed aperture (PubMed:32251414). Mediates the calcium-activated hydrogencarbonate movement and participates in colonic hydrogencarbonate secretion concomitant with mucin secretion (By similarity). In non-pigmented epithelium (NPE), mediates the efflux of intracellular L-glutamate; binding of intracellular L-glutamate activates and open both the neck and the aperture of the channel, leading to L-glutamate exit promoting chloride influx movement from the extracellular side in trans (By similarity). Also exhibits a directional permeability for intracellular glutamine, in a similar manner as for L-glutamate (By similarity).[UniProtKB:Q8BGM5][UniProtKB:Q8NFU1] See Also Glutamine synthetase 3D structures

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