› 2uzz

X-ray diffraction
3.2Å resolution

X-ray structure of N-methyl-L-tryptophan oxidase (MTOX)

Released:
DOI: 10.2210/pdb2uzz/pdb
PDB entry 2uzz coloured by chain, front view.
PDB entry 2uzz coloured by chain, side view.
PDB entry 2uzz coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity.
Ilari A, Bonamore A, Franceschini S, Fiorillo A, Boffi A, Colotti G
Proteins 71 2065-75 (2008)
PMID: 18186483

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-methyl-L-tryptophan oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 372 amino acids
Theoretical weight: 40.99 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40874 (Residues: 1-372; Coverage: 100%)
Gene names: JW1046, b1059, solA
Sequence domains: FAD dependent oxidoreductase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FAD 4 x FAD
Ligand NA 4 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P2
Unit cell:
a: 88.188Å b: 89.809Å c: 91.915Å
α: 90° β: 104.75° γ: 90°
R-values:
R R work R free
0.24 0.236 0.313
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

What's in a covalent bond? On the role and formation of covalently bound flavin cofactors.
Heuts et al. (2009)
7 other articles

2 mentions without citation

Pleiotropic impact of a single lysine mutation on biosynthesis of and catalysis by N-methyltryptophan oxidase.
Bruckner et al. (2011)
1 more