› 5wmk

X-ray diffraction
1.4Å resolution

Arabidopsis thaliana Prephenate Aminotransferase double mutant- T84V K169V

Released:
DOI: 10.2210/pdb5wmk/pdb
PDB entry 5wmk coloured by chain, front view.
PDB entry 5wmk coloured by chain, side view.
PDB entry 5wmk 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 Chain: A
Molecule details ›
Chain: A
Length: 475 amino acids
Theoretical weight: 51.02 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

2 bound ligands:
Ligand MLI 1 x MLI
Ligand BO3 1 x BO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 116.498Å b: 64.891Å c: 51.933Å
α: 90° β: 105.87° γ: 90°
R-values:
R R work R free
0.161 0.161 0.178
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