› 7mya

X-ray diffraction
1.56Å resolution

Structure of proline utilization A with the FAD covalently-modified by 1,3-dithiolane

Released:
DOI: 10.2210/pdb7mya/pdb
Model geometry
Fit model/data
PDB entry 7mya coloured by chain, front view.
PDB entry 7mya coloured by chain, side view.
PDB entry 7mya coloured by chain, top view.
Source organism: Sinorhizobium meliloti SM11
Primary publication:
Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles.
Campbell AC, Prater AR, Bogner AN, Quinn TP, Gates KS, Becker DF, Tanner JJ
ACS Chem Biol 16 2268-2279 (2021)
PMID: 34542291

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 (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-123681 (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 NAD 2 x NAD
6 bound ligands:
Ligand UJJ 2 x UJJ
Ligand MG 2 x MG
Ligand SO4 7 x SO4
Ligand PGE 4 x PGE
Ligand PEG 3 x PEG
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 101.176Å b: 101.884Å c: 125.931Å
α: 90° β: 106.49° γ: 90°
R-values:
R R work R free
0.177 0.176 0.205
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase.
Bogner et al. (2022)
1 more

1 mention without citation

Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles.
Campbell et al. (2021)