› 3haz

X-ray diffraction
2.1Å resolution

Crystal structure of bifunctional proline utilization A (PutA) protein

Released:
DOI: 10.2210/pdb3haz/pdb
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PDB entry 3haz coloured by chain, front view.
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Source organism: Bradyrhizobium diazoefficiens USDA 110
Primary publication:
Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum.
Srivastava D, Schuermann JP, White TA, Krishnan N, Sanyal N, Hura GL, Tan A, Henzl MT, Becker DF, Tanner JJ
Proc Natl Acad Sci U S A 107 2878-83 (2010)
PMID: 20133651

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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183542 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PutA Chains: A, B
Molecule details ›
Chains: A, B
Length: 1001 amino acids
Theoretical weight: 107.7 KDa
Source organism: Bradyrhizobium diazoefficiens USDA 110
Expression system: Escherichia coli
UniProt:
  • Canonical: Q89E26 (Residues: 1-999; Coverage: 100%)
Gene name: putA
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand SO4 13 x SO4
Ligand GOL 6 x GOL
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: C2
Unit cell:
a: 166.763Å b: 195.846Å c: 108.68Å
α: 90° β: 121.48° γ: 90°
R-values:
R R work R free
0.202 0.2 0.233
Expression system: Escherichia coli

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Citations

4 review citations

Flavin redox switching of protein functions.
Becker et al. (2011)
3 more

16 mentions without citation

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

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