› 4ppu

X-ray diffraction
2.3Å resolution

Crystal Structure of AtCM1 with Tyrosine Bound in Allosteric Site

Released:
DOI: 10.2210/pdb4ppu/pdb
PDB entry 4ppu coloured by chain, front view.
PDB entry 4ppu coloured by chain, side view.
PDB entry 4ppu coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural evolution of differential amino acid effector regulation in plant chorismate mutases.
Westfall CS, Xu A, Jez JM
J Biol Chem 289 28619-28 (2014)
PMID: 25160622

Function and Biology Details

Reaction catalysed: 
Chorismate = prephenate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154859 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate mutase 1, chloroplastic Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 31.64 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42738 (Residues: 65-340; Coverage: 81%)
Gene names: At3g29200, CM1, MXO21.4
Structure domains: Chorismate mutase, AroQ class superfamily, eukaryotic

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R32
Unit cell:
a: 99.859Å b: 99.859Å c: 156.277Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.162 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

A familiar ring to it: biosynthesis of plant benzoic acids.
Widhalm et al. (2015)
1 more

1 mention without citation

Structural evolution of differential amino acid effector regulation in plant chorismate mutases.
Westfall et al. (2014)