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Chemistry of ion coordination and hydration revealed by a K + channel-Fab complex at 2.0 resolution
Ist Teil von
Nature (London), 2001-11, Vol.414 (6859), p.43-48
Ort / Verlag
London: Nature Publishing
Erscheinungsjahr
2001
Link zum Volltext
Quelle
EBSCOhost Psychology and Behavioral Sciences Collection
Beschreibungen/Notizen
Ion transport proteins must remove an ion's hydration shell to coordinate the ion selectively on the basis of its size and charge. To discover how the K+ channel solves this fundamental aspect of ion conduction, we solved the structure of the KcsA K+ channel in complex with a monoclonal Fab antibody fragment at 2.0 A resolution. Here we show how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entryway. Carbonyl oxygen atoms within the selectivity filter form a very similar square antiprism around each K+ binding site, as if to mimic the waters of hydration. The selectivity filter changes its ion coordination structure in low K+ solutions. This structural change is crucial to the operation of the selectivity filter in the cellular context, where the K+ ion concentration near the selectivity filter varies in response to channel gating.