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TitleStructural Titration of Slo2.2, a Na-Dependent K Channel.
Journal, issue, pagesCell, Vol. 168, Issue 3, Page 390-399.e11, Year 2017
Publish dateJan 26, 2017
AuthorsRichard K Hite / Roderick MacKinnon /
PubMed AbstractThe stable structural conformations that occur along the complete reaction coordinate for ion channel opening have never been observed. In this study, we describe the equilibrium ensemble of ...The stable structural conformations that occur along the complete reaction coordinate for ion channel opening have never been observed. In this study, we describe the equilibrium ensemble of structures of Slo2.2, a neuronal Na-activated K channel, as a function of the Na concentration. We find that Slo2.2 exists in multiple closed conformations whose relative occupancies are independent of Na concentration. An open conformation emerges from an ensemble of closed conformations in a highly Na-dependent manner, without evidence of Na-dependent intermediates. In other words, channel opening is a highly concerted, switch-like process. The midpoint of the structural titration matches that of the functional titration. A maximum open conformation probability approaching 1.0 and maximum functional open probability approaching 0.7 imply that, within the class of open channels, there is a subclass that is not permeable to ions.
External linksCell / PubMed:28111072 / PubMed Central
MethodsEM (single particle)
Resolution3.76 Å
Structure data

8515

5u70

EMDB-8515, PDB-5u70:
Chicken Slo2.2 in an open conformation vitrified in the presence of 300 mM NaCl
Method: EM (single particle) / Resolution: 3.76 Å

8517

5u76

EMDB-8517, PDB-5u76:
Chicken Slo2.2 in a closed conformation vitrified in the presence of 300 mM NaCl
Method: EM (single particle) / Resolution: 3.76 Å

Source
  • gallus gallus (chicken)
KeywordsTRANSPORT PROTEIN / Ion channel / potassium channel

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