› 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 6x9b coloured by chain and viewed from the front.
PDB 6x9b coloured by chain and viewed from the side.
PDB 6x9b coloured by chain and viewed from the top.
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:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric
homo dimer (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

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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)
2 other articles