› 5ux5

X-ray diffraction
2.7Å resolution

Structure of Proline Utilization A (PutA) from Corynebacterium freiburgense

Released:
DOI: 10.2210/pdb5ux5/pdb
PDB entry 5ux5 coloured by chain, front view.
PDB entry 5ux5 coloured by chain, side view.
PDB entry 5ux5 coloured by chain, top view.
Source organism: Corynebacterium freiburgense
Primary publication:
Structure and characterization of a class 3B proline utilization A: Ligand-induced dimerization and importance of the C-terminal domain for catalysis.
Korasick DA, Gamage TT, Christgen S, Stiers KM, Beamer LJ, Henzl MT, Becker DF, Tanner JJ
J Biol Chem 292 9652-9665 (2017)
PMID: 28420730

Function and Biology Details

Reaction catalysed: 
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103872 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-glutamate gamma-semialdehyde dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1076 amino acids
Theoretical weight: 119.39 KDa
Source organism: Corynebacterium freiburgense
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1X8XLF1 (Residues: 1-1076; Coverage: 100%)
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD

Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P1
Unit cell:
a: 84.959Å b: 116.36Å c: 140.734Å
α: 71.48° β: 89.68° γ: 83.42°
R-values:
R R work R free
0.185 0.183 0.236
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Role of Proline in Pathogen and Host Interactions.
Christgen et al. (2019)
1 more

3 mentions without citation

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