4KFC
Crystal structure of a hyperactive mutant of response regulator KdpE complexed to its promoter DNA
Summary for 4KFC
| Entry DOI | 10.2210/pdb4kfc/pdb |
| Descriptor | KDP operon transcriptional regulatory protein KdpE, Promoter DNA, ... (4 entities in total) |
| Functional Keywords | receiver domain, dna-binding domain, transcription regulator-dna complex, transcription regulator/dna |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm: P21866 |
| Total number of polymer chains | 4 |
| Total formula weight | 69318.34 |
| Authors | Kumar, S.,Narayanan, A.,Yernool, D.A. (deposition date: 2013-04-26, release date: 2014-02-19, Last modification date: 2023-09-20) |
| Primary citation | Narayanan, A.,Kumar, S.,Evrard, A.N.,Paul, L.N.,Yernool, D.A. An asymmetric heterodomain interface stabilizes a response regulator-DNA complex. Nat Commun, 5:3282-3282, 2014 Cited by PubMed 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. PubMed: 24526190DOI: 10.1038/ncomms4282 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.53 Å) |
Structure validation
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