› 3e2r

X-ray diffraction
1.85Å resolution

Crystal Structure PutA86-630 Mutant Y540S Complexed with L-tetrahydro-2-furoic acid

Released:
DOI: 10.2210/pdb3e2r/pdb
PDB entry 3e2r coloured by chain, front view.
PDB entry 3e2r coloured by chain, side view.
PDB entry 3e2r coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate.
Ostrander EL, Larson JD, Schuermann JP, Tanner JJ
Biochemistry 48 951-9 (2009)
PMID: 19140736

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:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PutA Chain: A
Molecule details ›
Chain: A
Length: 551 amino acids
Theoretical weight: 61.38 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P09546 (Residues: 86-630; Coverage: 41%)
Gene names: JW0999, b1014, poaA, putA
Sequence domains:
Structure domains: TIM Barrel

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
3 bound ligands:
Ligand TFB 1 x TFB
Ligand CIT 1 x CIT
Ligand 1PE 2 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: I222
Unit cell:
a: 72.648Å b: 140.102Å c: 146.665Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.227
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural Biology of Proline Catabolic Enzymes.
Tanner JJ. (2019)
2 more

3 mentions without citation

A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate.
Ostrander et al. (2009)
2 more