› 4uhk

X-ray diffraction
2.6Å resolution

Crystal structure of the receiver domain of CpxR from E. coli (phosphorylated)

Released:
DOI: 10.2210/pdb4uhk/pdb
PDB entry 4uhk coloured by chain, front view.
PDB entry 4uhk coloured by chain, side view.
PDB entry 4uhk coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural Coupling between Autokinase and Phosphotransferase Reactions in a Bacterial Histidine Kinase.
Mechaly AE, Soto Diaz S, Sassoon N, Buschiazzo A, Betton JM, Alzari PM
Structure 25 939-944.e3 (2017)
PMID: 28552574

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142420 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcriptional regulatory protein CpxR Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 136 amino acids
Theoretical weight: 15.64 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE88 (Residues: 1-123; Coverage: 53%)
Gene names: JW3883, b3912, cpxR, yiiA
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand MG 3 x MG
1 modified residue:
Ligand PHD 3 x PHD

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 86.831Å b: 74.144Å c: 76.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.233
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural insights into the signalling mechanisms of two-component systems.
Jacob-Dubuisson et al. (2018)
14 other articles

1 mention without citation

Experimental Evolution of Copper Resistance in Escherichia coli Produces Evolutionary Trade-Offs in the Antibiotics Chloramphenicol, Bacitracin, and Sulfonamide.
Boyd et al. (2022)