Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.

Journal article

Potassium channels allow the selective flow of K(+) ions across membranes. In response to external gating signals, the potassium channel can move reversibly through a series of structural conformations from a closed to an open state. 2D crystals of the inwardly rectifying K(+) channel KirBac3.1 from Magnetospirillum magnetotacticum have been captured in two distinct conformations, providing "snap shots" of the gating process. Analysis by electron cryomicroscopy of these KirBac3.1 crystals has...

Expand abstract

Authors: Kuo, A; Domene, C; Johnson, L; Doyle, D; Vénien-Bryan, C

• Journal: Structure (London, England : 1993)
• Volume: 13
• Issue: 10
• Pages: 1463-72
• Publication date: 2005-01-01
• ISSN: 0969-2126
• Language: English
• Subjects: Cryoelectron Microscopy; ultrastructure; chemistry; Crystallography, X-Ray; genetics; Protein Structure, Quaternary; Protein Structure, Secondary; Cloning, Molecular; Sequence Homology, Amino Acid; Amino Acids, Aromatic; Lipid Bilayers; Dimerization; Magnetospirillum; Amino Acid Sequence; DNA, Bacterial; Molecular Sequence Data; Protein Conformation; Models, Molecular; Potassium Channels, Inwardly Rectifying