Research ArticleStructural Biology

Structural insights into the signal transduction mechanism of the K+-sensing two-component system KdpDE

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Science Signaling  04 Aug 2020:
Vol. 13, Issue 643, eaaz2970
DOI: 10.1126/scisignal.aaz2970

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More than just DNA binding

Specificity between binding partners in bacterial two-component systems, which comprise a histidine kinase sensor and a downstream response regulator, is critical for stimulating appropriate cellular responses to environmental stimuli. Xie et al. solved the crystal structure of the catalytic module of the histidine kinase KdpD in complex with its cognate response regulator KdpE. This structure, in combination with biochemical assays and functional experiments, demonstrated that the DNA binding domain of KdpE contributed to the specific interaction between these partners by interacting with the catalytic domain of KdpD. The KdpD catalytic domain competed with DNA for binding to KdpE, and this interaction was important for the ability of KdpD to stimulate KdpE activity. These findings illustrate a mechanism through which binding specificity may evolve to ensure cognate interactions in two-component systems.

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