› 2g37

X-ray diffraction
2Å resolution

Structure of Thermus thermophilus L-proline dehydrogenase

Released:
DOI: 10.2210/pdb2g37/pdb
PDB entry 2g37 coloured by chain, front view.
PDB entry 2g37 coloured by chain, side view.
PDB entry 2g37 coloured by chain, top view.
Source organism: Thermus thermophilus HB27
Primary publication:
Structure and kinetics of monofunctional proline dehydrogenase from Thermus thermophilus.
White TA, Krishnan N, Becker DF, Tanner JJ
J Biol Chem 282 14316-27 (2007)
PMID: 17344208

Function and Biology Details

Reaction catalysed: 
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 327 amino acids
Theoretical weight: 38.05 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72IB8 (Residues: 1-307; Coverage: 100%)
Gene name: TT_C1214
Sequence domains: Proline dehydrogenase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand MPD 4 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P212121
Unit cell:
a: 82.067Å b: 89.59Å c: 94.316Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.231
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Proline mechanisms of stress survival.
Liang et al. (2013)
12 more

8 mentions without citation

Substrate channeling in proline metabolism.
Arentson et al. (2012)
7 more