› 5v0s

X-ray diffraction
2.01Å resolution

Crystal structure of the ACT domain of prephenate dehydrogenase tyrA from Bacillus anthracis

Released:
DOI: 10.2210/pdb5v0s/pdb
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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:
  • not assigned
Biological process:
  • not assigned
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: 69 amino acids
Theoretical weight: 7.93 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q81P63 (Residues: 307-375; Coverage: 18%)
Gene names: GBAA_2954, tyrA
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand CA 2 x CA
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P6522
Unit cell:
a: 48.07Å b: 48.07Å c: 233.395Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.171 0.232
Expression system: Escherichia coli

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Citations

2 citation 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 more

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)

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