› 2gpe

X-ray diffraction
1.9Å resolution

Structure of the DNA-binding domain of E. Coli Proline Utilization A (PUTA)

Released:
DOI: 10.2210/pdb2gpe/pdb
PDB entry 2gpe coloured by chain, front view.
PDB entry 2gpe coloured by chain, side view.
PDB entry 2gpe coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition.
Larson JD, Jenkins JL, Schuermann JP, Zhou Y, Becker DF, Tanner JJ
Protein Sci 15 2630-41 (2006)
PMID: 17001030

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:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PutA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 52 amino acids
Theoretical weight: 5.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P09546 (Residues: 1-52; Coverage: 4%)
Gene names: JW0999, b1014, poaA, putA
Sequence domains: PutA, RHH domain
Structure domains: Met repressor-like

Ligands and Environments

1 bound ligand:
Ligand IMD 4 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P41212
Unit cell:
a: 55.731Å b: 55.731Å c: 125.019Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.249
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Proline mechanisms of stress survival.
Liang et al. (2013)
4 more

12 mentions without citation

Structural biology of proline catabolism.
Tanner JJ. (2008)
11 more