› 6u60

X-ray diffraction
2.1Å resolution

Crystal structure of prephenate dehydrogenase tyrA from Bacillus anthracis in complex with NAD and L-tyrosine

Released:
DOI: 10.2210/pdb6u60/pdb
PDB entry 6u60 coloured by chain, front view.
PDB entry 6u60 coloured by chain, side view.
PDB entry 6u60 coloured by chain, top view.
Source organism: Bacillus anthracis
Primary publication:
Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain.
Shabalin IG, Gritsunov A, Hou J, Sławek J, Miks CD, Cooper DR, Minor W, Christendat D
FEBS J 287 2235-2255 (2020)
PMID: 31750992

Function and Biology Details

Reaction catalysed: 
Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prephenate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 381 amino acids
Theoretical weight: 42.71 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q81P63 (Residues: 1-378; Coverage: 100%)
Gene names: GBAA_2954, tyrA
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
2 bound ligands:
Ligand TYR 2 x TYR
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21212
Unit cell:
a: 106.85Å b: 81.003Å c: 83.597Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.16 0.22
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Intragenic suppressors unravel the role of the SCREAM ACT-like domain for bHLH partner selectivity in stomatal development.
Seo et al. (2022)

1 mention without citation

Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain.
Shabalin et al. (2020)