6oly | pdb_00006oly

Full-length MthK channel at 3.1 angstrom resolution

spinqualitylabelsall models 6oly, resolution 3.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6oly is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MTHK_METTH] Calcium-gated potassium channel. Publication Abstract from PubMed Potassium channels are presumed to have two allosterically coupled gates, the activation gate and the selectivity filter gate, that control channel opening, closing, and inactivation. However, the molecular mechanism of how these gates regulate K(+ )ion flow through the channel remains poorly understood. An activation process, occurring at the selectivity filter, has been recently proposed for several potassium channels. Here, we use X-ray crystallography and extensive molecular dynamics simulations, to study ion permeation through a potassium channel MthK, for various opening levels of both gates. We find that the channel conductance is controlled at the selectivity filter, whose conformation depends on the activation gate. The crosstalk between the gates is mediated through a collective motion of channel helices, involving hydrophobic contacts between an isoleucine and a conserved threonine in the selectivity filter. We propose a gating model of selectivity filter-activated potassium channels, including pharmacologically relevant two-pore domain (K2P) and big potassium (BK) channels. Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling.,Kopec W, Rothberg BS, de Groot BL Nat Commun. 2019 Nov 26;10(1):5366. doi: 10.1038/s41467-019-13227-w. PMID:31772184 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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