1KPK
Crystal Structure of the ClC Chloride Channel from E. coli
Summary for 1KPK
| Entry DOI | 10.2210/pdb1kpk/pdb |
| Related | 1KPL |
| Descriptor | putative channel transporter (1 entity in total) |
| Functional Keywords | helical membrane protein, homodimer, membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Multi-pass membrane protein (Probable): P37019 |
| Total number of polymer chains | 6 |
| Total formula weight | 302342.41 |
| Authors | Dutzler, R.,Campbell, E.B.,Cadene, M.,Chait, B.T.,MacKinnon, R. (deposition date: 2001-12-31, release date: 2002-01-23, Last modification date: 2024-02-14) |
| Primary citation | Dutzler, R.,Campbell, E.B.,Cadene, M.,Chait, B.T.,MacKinnon, R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature, 415:287-294, 2002 Cited by PubMed Abstract: The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. Genetic defects in ClC Cl- channels underlie several familial muscle and kidney diseases. Here we present the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 A, respectively. Both structures reveal two identical pores, each pore being formed by a separate subunit contained within a homodimeric membrane protein. Individual subunits are composed of two roughly repeated halves that span the membrane with opposite orientations. This antiparallel architecture defines a selectivity filter in which a Cl- ion is stabilized by electrostatic interactions with alpha-helix dipoles and by chemical coordination with nitrogen atoms and hydroxyl groups. These findings provide a structural basis for further understanding the function of ClC Cl- channels, and establish the physical and chemical basis of their anion selectivity. PubMed: 11796999DOI: 10.1038/415287a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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