› 6d6d

X-ray diffraction
1.7Å resolution

The structure of ligand binding domain of LasR in complex with TP-1 homolog, compound 13

Released:
DOI: 10.2210/pdb6d6d/pdb
PDB entry 6d6d coloured by chain, front view.
PDB entry 6d6d coloured by chain, side view.
PDB entry 6d6d coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structural and Biochemical Studies of Non-native Agonists of the LasR Quorum-Sensing Receptor Reveal an L3 Loop "Out" Conformation for LasR.
O'Reilly MC, Dong SH, Rossi FM, Karlen KM, Kumar RS, Nair SK, Blackwell HE
Cell Chem Biol 25 1128-1139.e3 (2018)
PMID: 30033130

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcriptional activator protein LasR Chains: A, B
Molecule details ›
Chains: A, B
Length: 169 amino acids
Theoretical weight: 18.91 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: P25084 (Residues: 1-169; Coverage: 71%)
Gene names: PA1430, lasR
Sequence domains: Autoinducer binding domain
Structure domains: Transcription factor LuxR-like, autoinducer-binding domain

Ligands and Environments

1 bound ligand:
Ligand FY7 2 x FY7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 43.48Å b: 64.2Å c: 53.92Å
α: 90° β: 92.32° γ: 90°
R-values:
R R work R free
0.23 0.228 0.274
Expression system: Escherichia coli

Quick links

Citations

22 citation in other articles

Structural determinants driving homoserine lactone ligand selection in the Pseudomonas aeruginosa LasR quorum-sensing receptor.
McCready et al. (2019)
21 more

1 mention without citation

Structural and Biochemical Studies of Non-native Agonists of the LasR Quorum-Sensing Receptor Reveal an L3 Loop "Out" Conformation for LasR.
O'Reilly et al. (2018)