› 1tt8

X-ray diffraction
1Å resolution

CHORISMATE LYASE WITH PRODUCT, 1.0 A RESOLUTION

Released:
DOI: 10.2210/pdb1tt8/pdb
PDB entry 1tt8 coloured by chain, front view.
PDB entry 1tt8 coloured by chain, side view.
PDB entry 1tt8 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural analysis of ligand binding and catalysis in chorismate lyase.
Smith N, Roitberg AE, Rivera E, Howard A, Holden MJ, Mayhew M, Kaistha S, Gallagher DT
Arch Biochem Biophys 445 72-80 (2006)
PMID: 16343413

Function and Biology Details

Reaction catalysed: 
Chorismate = 4-hydroxybenzoate + pyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate pyruvate-lyase Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.64 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P26602 (Residues: 2-165; Coverage: 99%)
Gene names: JW5713, b4039, ubiC
Sequence domains: Chorismate lyase
Structure domains: Chorismate lyase-like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P1
Unit cell:
a: 31.315Å b: 33.849Å c: 39.776Å
α: 67.57° β: 87.83° γ: 65.66°
R-values:
R R work R free
0.12 0.123 0.153
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biosynthesis and physiology of coenzyme Q in bacteria.
Aussel et al. (2014)
1 more

6 mentions without citation

Dynamic allostery can drive cold adaptation in enzymes.
Saavedra et al. (2018)
5 more