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• W2103770142 abstract "KirBac channels are the bacterial homologs of mammalian inwardly rectifying potassium (Kir) channels. All available structures are closed at the helix bundle crossing, but the crystal structure of an open-state KirBac channel now indicates how opening of the primary activation gate may be physically coupled to a rotational twist in the cytoplasmic domain. KirBac channels are prokaryotic homologs of mammalian inwardly rectifying (Kir) potassium channels, and recent crystal structures of both Kir and KirBac channels have provided major insight into their unique structural architecture. However, all of the available structures are closed at the helix bundle crossing, and therefore the structural mechanisms that control opening of their primary activation gate remain unknown. In this study, we engineered the inner pore-lining helix (TM2) of KirBac3.1 to trap the bundle crossing in an apparently open conformation and determined the crystal structure of this mutant channel to 3.05 Å resolution. Contrary to previous speculation, this new structure suggests a mechanistic model in which rotational 'twist' of the cytoplasmic domain is coupled to opening of the bundle-crossing gate through a network of inter- and intrasubunit interactions that involve the TM2 C-linker, slide helix, G-loop and the CD loop." @default.
• W2103770142 created "2016-06-24" @default.
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• W2103770142 date "2012-01-08" @default.
• W2103770142 modified "2023-10-15" @default.
• W2103770142 title "Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating" @default.
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• W2103770142 doi "https://doi.org/10.1038/nsmb.2208" @default.
• W2103770142 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3272479" @default.
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• W2103770142 hasPublicationYear "2012" @default.
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