› 5wml

X-ray diffraction
2.1Å resolution

Arabidopsis thaliana Prephenate Aminotransferase mutant- K306A

Released:
DOI: 10.2210/pdb5wml/pdb
PDB entry 5wml coloured by chain, front view.
PDB entry 5wml coloured by chain, side view.
PDB entry 5wml coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis.
Holland CK, Berkovich DA, Kohn ML, Maeda H, Jez JM
Plant J 94 304-314 (2018)
PMID: 29405514

Function and Biology Details

Reactions catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-arogenate + oxaloacetate = prephenate + L-aspartate


L-arogenate + 2-oxoglutarate = prephenate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193463 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 475 amino acids
Theoretical weight: 51 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SIE1 (Residues: 1-475; Coverage: 100%)
Gene names: AAT, At2g22250, MEE17, PAT, T26C19.9
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 2 x PMP
1 bound ligand:
Ligand GLU 2 x GLU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 51.813Å b: 60.117Å c: 66.734Å
α: 74.78° β: 76.7° γ: 83.92°
R-values:
R R work R free
0.156 0.153 0.212
Expression system: Escherichia coli

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Citations

1 review citation

Harnessing evolutionary diversification of primary metabolism for plant synthetic biology.
Maeda HA. (2019)
6 other articles