2g5f

X-ray diffraction
1.8Å resolution

The structure of MbtI from Mycobacterium Tuberculosis, the first enzyme in the synthesis of Mycobactin, reveals it to be a salicylate synthase

Released:

Function and Biology Details

Reactions catalysed:
Isochorismate = salicylate + pyruvate
Chorismate = isochorismate
Chorismate = prephenate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161436 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Salicylate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 450 amino acids
Theoretical weight: 48.78 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WFX1 (Residues: 2-450; Coverage: 100%)
Gene names: Rv2386c, mbtI, trpE2
Sequence domains: chorismate binding enzyme
Structure domains: Anthranilate synthase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 51.82Å b: 163.37Å c: 194.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.24
Expression system: Escherichia coli