› 4a72

X-ray diffraction
2.4Å resolution

Crystal structure of the omega transaminase from Chromobacterium violaceum in a mixture of apo and PLP-bound states

Released:
DOI: 10.2210/pdb4a72/pdb
PDB entry 4a72 coloured by chain, front view.
PDB entry 4a72 coloured by chain, side view.
PDB entry 4a72 coloured by chain, top view.
Source organism: Chromobacterium violaceum
Primary publication:
Crystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP.
Humble MS, Cassimjee KE, Håkansson M, Kimbung YR, Walse B, Abedi V, Federsel HJ, Berglund P, Logan DT
FEBS J 279 779-92 (2012)
PMID: 22268978

Function and Biology Details

Reaction catalysed: 
L-alanine + 3-oxopropanoate = pyruvate + beta-alanine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181841 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative 8-amino-7-oxononanoate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 459 amino acids
Theoretical weight: 51.28 KDa
Source organism: Chromobacterium violaceum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7NWG4 (Residues: 1-459; Coverage: 100%)
Gene name: CV_2025
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P1
Unit cell:
a: 61.35Å b: 62.12Å c: 119.24Å
α: 105.27° β: 90.66° γ: 104.43°
R-values:
R R work R free
0.176 0.173 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis.
Kohls et al. (2014)
3 more

5 mentions without citation

Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement.
Kwon et al. (2019)
4 more