Crystal structure of the potassium channel KirBac1.1 in the closed state.
The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.
Kuo
Anling
A
University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK.
Gulbis
Jacqueline M
JM
Antcliff
Jennifer F
JF
Rahman
Tahmina
T
Lowe
Edward D
ED
Zimmer
Jochen
J
Cuthbertson
Jonathan
J
Ashcroft
Frances M
FM
Ezaki
Takayuki
T
Doyle
Declan A
DA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D016957:Burkholderia pseudomallei / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D057927:Hydrophobic and Hydrophilic Interactions; D015640:Ion Channel Gating; D017136:Ion Transport; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011188:Potassium / Q000378:metabolism; D024661:Potassium Channels, Inwardly Rectifying / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D024661:Potassium Channels, Inwardly Rectifying; D011188:Potassium