3E86
High resolution Crystal Structure of the open NaK channel pore
Summary for 3E86
| Entry DOI | 10.2210/pdb3e86/pdb |
| Related | 3E83 3E89 3E8B 3E8F 3E8G 3E8H |
| Descriptor | Potassium channel protein, (4S)-2-METHYL-2,4-PENTANEDIOL, CESIUM ION, ... (6 entities in total) |
| Functional Keywords | non-selective cation channel, membrane protein, tetrameric cation channel family, 2-transmembrane helix channels, ionic channel |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 2 |
| Total formula weight | 22047.27 |
| Authors | |
| Primary citation | Alam, A.,Jiang, Y. High-resolution structure of the open NaK channel Nat.Struct.Mol.Biol., 16:30-34, 2009 Cited by PubMed Abstract: We report the crystal structure of the nonselective cation channel NaK from Bacillus cereus at a resolution of 1.6 A. The structure reveals the intracellular gate in an open state, as opposed to the closed form reported previously, making NaK the only channel for which the three-dimensional structures of both conformations are known. Channel opening follows a conserved mechanism of inner helix bending using a flexible glycine residue, the gating hinge, seen in MthK and most other tetrameric cation channels. Additionally, distinct inter and intrasubunit rearrangements involved in channel gating are seen and characterized for the first time along with inner helix twisting motions. Furthermore, we identify a residue deeper within the cavity of the channel pore, Phe92, which is likely to form a constriction point within the open pore, restricting ion flux through the channel. Mutating this residue to alanine causes a subsequent increase in ion-conduction rates as measured by (86)Rb flux assays. The structures of both the open and closed conformations of the NaK channel correlate well with those of equivalent K(+) channel conformations, namely MthK and KcsA, respectively. PubMed: 19098917DOI: 10.1038/nsmb.1531 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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