› 4o8a

X-ray diffraction
2Å resolution

First structure of a proline utilization A proline dehydrogenase domain

Released:
DOI: 10.2210/pdb4o8a/pdb
PDB entry 4o8a coloured by chain, front view.
PDB entry 4o8a coloured by chain, side view.
PDB entry 4o8a coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein.
Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ
Nat Struct Biol 10 109-14 (2003)
PMID: 12514740

Function and Biology Details

Reactions catalysed: 
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-531216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PutA Chain: A
Molecule details ›
Chain: A
Length: 687 amino acids
Theoretical weight: 76.1 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P09546 (Residues: 1-669; Coverage: 51%)
Gene names: JW0999, b1014, poaA, putA
Sequence domains:
Structure domains: TIM Barrel

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
Ligand 2OP 1 x 2OP
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: I222
Unit cell:
a: 72.62Å b: 140.43Å c: 145.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.219
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Single-gene disorders: what role could moonlighting enzymes play?
Sriram et al. (2005)
14 more

4 mentions without citation

Structure, function, and mechanism of proline utilization A (PutA).
Liu et al. (2017)
3 more