SNAP output for PDB entry 4kny [SNAP web server]

PDB-id

4kny; SNAP-derived features in text and JSON formats; DNAproDB

Class

transcription regulator-DNA

Method

X-ray (2.945 Å)

Summary

Crystal structure of the response regulator kdpe complexed to DNA in an active-like conformation

Reference

Narayanan A, Kumar S, Evrard AN, Paul LN, Yernool DA (2014): "An asymmetric heterodomain interface stabilizes a response regulator-DNA complex." Nat Commun, 5, 3282. doi: 10.1038/ncomms4282.

Abstract

Two-component signal transduction systems consist of pairs of histidine kinases and response regulators, which mediate adaptive responses to environmental cues. Most activated response regulators regulate transcription by binding tightly to promoter DNA via a phosphorylation-triggered inactive-to-active transition. The molecular basis for formation of stable response regulator-DNA complexes that precede the assembly of RNA polymerases is unclear. Here, we present structures of DNA complexed with the response regulator KdpE, a member of the OmpR/PhoB family. The distinctively asymmetric complex in an active-like conformation reveals a unique intramolecular interface between the receiver domain (RD) and the DNA-binding domain (DBD) of only one of the two response regulators in the complex. Structure-function studies show that this RD-DBD interface is necessary to form stable complexes that support gene expression. The conservation of sequence and structure suggests that these findings extend to a large group of response regulators that act as transcription factors.