4l50

X-ray diffraction
2.1Å resolution

Crystal structures of the LsrR proteins complexed with phospho-AI-2 and its two different analogs reveal distinct mechanisms for ligand recognition

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcriptional regulator LsrR Chains: A, B
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 27.92 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P76141 (Residues: 53-317; Coverage: 84%)
Gene names: JW1505, b1512, lsrR, ydeW
Sequence domains: Putative sugar-binding domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P65
Unit cell:
a: 116.809Å b: 116.809Å c: 79.975Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.166 0.218
Expression system: Escherichia coli