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X-ray diffraction
1.58Å resolution

E. coli trp aporeporessor L75F mutant

Released:
DOI: 10.2210/pdb3ssx/pdb
PDB entry 3ssx coloured by chain, front view.
PDB entry 3ssx coloured by chain, side view.
PDB entry 3ssx coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Environment-dependent long-range structural distortion in a temperature-sensitive point mutant.
Carey J, Benoff B, Harish B, Yuan L, Lawson CL
Protein Sci 21 63-74 (2012)
PMID: 22057811

Function and Biology Details

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

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: N, R
Molecule details ›
Chains: N, R
Length: 107 amino acids
Theoretical weight: 12.27 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A881 (Residues: 2-108; Coverage: 99%)
Gene names: JW4356, b4393, rtrY, trpR
Sequence domains: Trp repressor protein
Structure domains: TrpR-like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P21
Unit cell:
a: 35.716Å b: 54.105Å c: 55.633Å
α: 90° β: 100.1° γ: 90°
R-values:
R R work R free
0.178 0.176 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of L-tryptophan.
Sprenger et al. (2021)

2 mentions without citation

Multiple helical conformations of the helix-turn-helix region revealed by NOE-restrained MD simulations of tryptophan aporepressor, TrpR.
Harish et al. (2017)
1 more