PDBsum entry 4l85

Transcription

PDB id: 4l85

Contents

Protein chains

116 a.a.

115 a.a.

120 a.a.

Metals

IOD ×35

Waters ×163

PDB id:

4l85

Name:

Transcription

Title:

Crystal structure of receiver domain of kdpe d52a mutant from e. Coli

Structure:

Kdp operon transcriptional regulatory protein kdpe. Chain: a, b, c. Fragment: response regulatory domain residues 3-121. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k-12. Gene: b0694, jw5096, kdpe. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.20Å R-factor: 0.176 R-free: 0.219

Authors:

S.Kumar,D.A.Yernool

Key ref:

A.Narayanan et al. (2014). An asymmetric heterodomain interface stabilizes a response regulator-DNA complex. Nat Commun, 5, 3282. PubMed id: 24526190 DOI: 10.1038/ncomms4282

Date:

15-Jun-13 Release date: 19-Feb-14

Protein chain

P21866  (KDPE_ECOLI) -  KDP operon transcriptional regulatory protein KdpE from Escherichia coli (strain K12)

Seq: 225 a.a.

Struc: 116 a.a.*

Protein chain

P21866  (KDPE_ECOLI) -  KDP operon transcriptional regulatory protein KdpE from Escherichia coli (strain K12)

Seq: 225 a.a.

Struc: 115 a.a.*

Protein chain

P21866  (KDPE_ECOLI) -  KDP operon transcriptional regulatory protein KdpE from Escherichia coli (strain K12)

Seq: 225 a.a.

Struc: 120 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C: E.C.?

DOI no: 10.1038/ncomms4282

Nat Commun 5:3282 (2014)

PubMed id: 24526190

An asymmetric heterodomain interface stabilizes a response regulator-DNA complex.

A.Narayanan, S.Kumar, A.N.Evrard, L.N.Paul, D.A.Yernool.

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.