› 2o99

X-ray diffraction
1.7Å resolution

The crystal structure of E.coli IclR C-terminal fragment in complex with glyoxylate

Released:
DOI: 10.2210/pdb2o99/pdb
PDB entry 2o99 coloured by chain, front view.
PDB entry 2o99 coloured by chain, side view.
PDB entry 2o99 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Glyoxylate and pyruvate are antagonistic effectors of the Escherichia coli IclR transcriptional regulator.
Lorca GL, Ezersky A, Lunin VV, Walker JR, Altamentova S, Evdokimova E, Vedadi M, Bochkarev A, Savchenko A
J Biol Chem 282 16476-91 (2007)
PMID: 17426033

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147756 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcriptional repressor IclR Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 182 amino acids
Theoretical weight: 20.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P16528 (Residues: 98-274; Coverage: 65%)
Gene names: JW3978, b4018, iclR
Sequence domains: Bacterial transcriptional regulator
Structure domains: Beta-Lactamase

Ligands and Environments

2 bound ligands:
Ligand EDO 4 x EDO
Ligand GOA 4 x GOA
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 53.538Å b: 81.483Å c: 154.693Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.261
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Coordination of microbial metabolism.
Chubukov et al. (2014)
8 more

2 mentions without citation

Molecular control of gene expression by Brucella BaaR, an IclR-type transcriptional repressor.
Herrou et al. (2018)
1 more