› 1wrs

Solution NMR

NMR STUDY OF HOLO TRP REPRESSOR

Released:
DOI: 10.2210/pdb1wrs/pdb
PDB entry 1wrs coloured by chain, ensemble of 15 models, front view.
PDB entry 1wrs coloured by chain, ensemble of 15 models, side view.
PDB entry 1wrs coloured by chain, ensemble of 15 models, top view.
Source organism: Escherichia coli
Primary publication:
Refined solution structures of the Escherichia coli trp holo- and aporepressor.
Zhao D, Arrowsmith CH, Jia X, Jardetzky O
J Mol Biol 229 735-46 (1993)
PMID: 8433368

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141677 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trp operon repressor Chains: R, S
Molecule details ›
Chains: R, S
Length: 105 amino acids
Theoretical weight: 12.04 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A881 (Residues: 4-108; Coverage: 97%)
Gene names: JW4356, b4393, rtrY, trpR
Sequence domains: Trp repressor protein
Structure domains: TrpR-like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores

Quick links

Citations

8 review citations

Is allostery an intrinsic property of all dynamic proteins?
Gunasekaran et al. (2004)
7 more

1 mention without citation

Internal dynamics of the tryptophan repressor (TrpR) and two functionally distinct TrpR variants, L75F-TrpR and A77V-TrpR, in their l-Trp-bound forms.
Tripet et al. (2011)