Crystal structure of the potassium channel KirBac1.1 in the closed state.

Journal article

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.

Authors: Kuo, A; Gulbis, J; Antcliff, J; Rahman, T; Lowe, E

• Publication status: Published
• Journal: Science (New York, N.Y.)
• Volume: 300
• Issue: 5627
• Pages: 1922-1926
• Publication date: 2003-06-01
• DOI: 10.1126/science.1085028
• EISSN: 1095-9203
• ISSN: 0036-8075
• Language: English
• Keywords: Hydrophobic and Hydrophilic Interactions; Protein Conformation; Protein Structure, Quaternary; Dimerization; Bacterial Proteins; Binding Sites; Protein Structure, Tertiary; Ion Channel Gating; Ion Transport; Crystallography, X-Ray; Burkholderia pseudomallei; Potassium Channels, Inwardly Rectifying; Crystallization; Protein Structure, Secondary; Molecular Sequence Data; Potassium; Models, Molecular; Amino Acid Sequence