› 3zop

X-ray diffraction
1.61Å resolution

Arg90Cit chorismate mutase of Bacillus subtilis at 1.6 A resolution

Released:
DOI: 10.2210/pdb3zop/pdb
PDB entry 3zop coloured by chain, front view.
PDB entry 3zop coloured by chain, side view.
PDB entry 3zop coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.
Burschowsky D, van Eerde A, Ökvist M, Kienhöfer A, Kast P, Hilvert D, Krengel U
Proc Natl Acad Sci U S A 111 17516-21 (2014)
PMID: 25422475

Function and Biology Details

Reaction catalysed: 
Chorismate = prephenate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148491 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate mutase AroH Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 127 amino acids
Theoretical weight: 14.52 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P19080 (Residues: 1-127; Coverage: 100%)
Gene names: BSU22690, aroH
Sequence domains: Chorismate mutase type I
Structure domains: RutC-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CIR 6 x CIR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 50.134Å b: 51.131Å c: 69.906Å
α: 97.84° β: 92.97° γ: 101.26°
R-values:
R R work R free
0.171 0.169 0.221
Expression system: Escherichia coli

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Citations

1 review citation

The ascent of man(made oxidoreductases).
Grayson et al. (2018)
10 other articles

1 mention without citation

Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.
Burschowsky et al. (2014)