› 2avx

Solution NMR

solution structure of E coli SdiA1-171

Released:
DOI: 10.2210/pdb2avx/pdb
PDB entry 2avx coloured by chain, ensemble of 20 models, front view.
PDB entry 2avx coloured by chain, ensemble of 20 models, side view.
PDB entry 2avx coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones.
Yao Y, Martinez-Yamout MA, Dickerson TJ, Brogan AP, Wright PE, Dyson HJ
J Mol Biol 355 262-73 (2006)
PMID: 16307757

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein SdiA Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 20.39 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P07026 (Residues: 1-171; Coverage: 71%)
Gene names: JW1901, b1916, sdiA
Sequence domains: Autoinducer binding domain
Structure domains: Transcription factor LuxR-like, autoinducer-binding domain

Ligands and Environments

1 bound ligand:
Ligand HTF 1 x HTF
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics simulated annealing
Expression system: Escherichia coli

Quick links

Citations

39 review citations

Bacterial quorum-sensing network architectures.
Ng et al. (2009)
38 more

4 mentions without citation

Structural basis of acyl-homoserine lactone-dependent signaling.
Churchill et al. (2011)
3 more