› 3kot

X-ray diffraction
1.9Å resolution

Structure of the Citrobacter freundii effector binding domain containing three amino acid substitutions: T103V, S221A and Y264F

Released:
DOI: 10.2210/pdb3kot/pdb
PDB entry 3kot coloured by chain, front view.
PDB entry 3kot coloured by chain, side view.
PDB entry 3kot 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: 24.65 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

1 bound ligand:
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 125.452Å b: 34.102Å c: 50.408Å
α: 90° β: 102.4° γ: 90°
R-values:
R R work R free
0.2 0.198 0.241
Expression system: Escherichia coli

Quick links

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)