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    Nat Struct Mol Biol. 2012 Jan 8;19(2):158-63. doi: 10.1038/nsmb.2208.

    Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating.

    Bavro VN, De Zorzi R, Schmidt MR, Muniz JR, Zubcevic L, Sansom MS, Vénien-Bryan C, Tucker SJ.

    Source

    1] Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK. [2] School of Immunity and Infection, University of Birmingham, Birmingham UK (V.N.B.); Institut de Minéralogie et de Physique des Milieux Condensés, Université Pierre et Marie Curie, Centre National de la Recherche Scientifique, UMR 7590, Paris, France (C.V.-B.). [3].

    Abstract

    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.

    PMID:
    22231399
    [PubMed - in process]
    PMCID:
    PMC3272479
    [Available on 2012/7/8]

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