› 6x9b

X-ray diffraction
1.46Å resolution

Structure of proline utilization A with cis-4-hydroxy-D-proline bound in the L-glutamate-gamma-semialdehyde dehydrogenase active site

Released:
DOI: 10.2210/pdb6x9b/pdb
PDB entry 6x9b coloured by chain, front view.
PDB entry 6x9b coloured by chain, side view.
PDB entry 6x9b coloured by chain, top view.
Source organism: Sinorhizobium meliloti SM11
Primary publication:
Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-γ-semialdehyde dehydrogenase active site of bifunctional proline utilization A.
Campbell AC, Bogner AN, Mao Y, Becker DF, Tanner JJ
Arch Biochem Biophys 698 108727 (2021)
PMID: 33333077

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:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123683 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PutA Chains: A, B
Molecule details ›
Chains: A, B
Length: 1235 amino acids
Theoretical weight: 131.96 KDa
Source organism: Sinorhizobium meliloti SM11
Expression system: Escherichia coli
UniProt:
  • Canonical: F7X6I3 (Residues: 1-1233; Coverage: 100%)
Gene names: SM11_chr0102, putA
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand NAD 2 x NAD
5 bound ligands:
Ligand PEG 1 x PEG
Ligand SO4 2 x SO4
Ligand MG 1 x MG
Ligand UYA 2 x UYA
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 100.89Å b: 101.92Å c: 126.2Å
α: 90° β: 106.44° γ: 90°
R-values:
R R work R free
0.195 0.194 0.22
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Aldehyde Dehydrogenase 2 as a Therapeutic Target in Oxidative Stress-Related Diseases: Post-Translational Modifications Deserve More Attention.
Gao et al. (2022)
3 other articles

1 mention without citation

Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-γ-semialdehyde dehydrogenase active site of bifunctional proline utilization A.
Campbell et al. (2021)