› 3kos

X-ray diffraction
1.83Å resolution

Structure of the AmpR effector binding domain from Citrobacter freundii

Released:
DOI: 10.2210/pdb3kos/pdb
PDB entry 3kos coloured by chain, front view.
PDB entry 3kos coloured by chain, side view.
PDB entry 3kos coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Crystal structure of the AmpR effector binding domain provides insight into the molecular regulation of inducible ampc beta-lactamase.
Balcewich MD, Reeve TM, Orlikow EA, Donald LJ, Vocadlo DJ, Mark BL
J Mol Biol 400 998-1010 (2010)
PMID: 20594961

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH-type transcriptional activator AmpR Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 25.06 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
  • Canonical: P12529 (Residues: 83-291; Coverage: 72%)
Gene name: ampR
Sequence domains: LysR substrate binding domain
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand MES 2 x MES
Ligand GOL 7 x GOL
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 125.28Å b: 34.19Å c: 49.98Å
α: 90° β: 102.77° γ: 90°
R-values:
R R work R free
0.174 0.17 0.202
Expression system: Escherichia coli

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Citations

13 review citations

Bacterial cell-wall recycling.
Johnson et al. (2013)
12 more

1 mention without citation

The β-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptide.
Vadlamani et al. (2015)