RRC ID 2542
Author Kuo A, Gulbis JM, Antcliff JF, Rahman T, Lowe ED, Zimmer J, Cuthbertson J, Ashcroft FM, Ezaki T, Doyle DA.
Title Crystal structure of the potassium channel KirBac1.1 in the closed state.
Journal Science
Abstract 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.
Volume 300(5627)
Pages 1922-6
Published 2003-6-20
DOI 10.1126/science.1085028
PII 1085028
PMID 12738871
MeSH Amino Acid Sequence Bacterial Proteins / chemistry* Bacterial Proteins / metabolism Binding Sites Burkholderia pseudomallei / chemistry* Crystallization Crystallography, X-Ray Dimerization Hydrophobic and Hydrophilic Interactions Ion Channel Gating* Ion Transport Models, Molecular Molecular Sequence Data Potassium / metabolism Potassium Channels, Inwardly Rectifying / chemistry* Potassium Channels, Inwardly Rectifying / metabolism Protein Conformation Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary
IF 41.846
Times Cited 615
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Pathogenic microorganisms