› 4nm9

X-ray diffraction
1.9Å resolution

Crystal structure of the resting state of proline utilization A (PutA) from Geobacter sulfurreducens PCA

Released:
DOI: 10.2210/pdb4nm9/pdb
PDB entry 4nm9 coloured by chain, front view.
PDB entry 4nm9 coloured by chain, side view.
PDB entry 4nm9 coloured by chain, top view.
Source organism: Geobacter sulfurreducens PCA
Primary publication:
Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site.
Singh H, Arentson BW, Becker DF, Tanner JJ
Proc Natl Acad Sci U S A 111 3389-94 (2014)
PMID: 24550478

Function and Biology Details

Reaction catalysed: 
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181012 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-glutamate gamma-semialdehyde dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 1005 amino acids
Theoretical weight: 112.32 KDa
Source organism: Geobacter sulfurreducens PCA
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q746X3 (Residues: 1-1004; Coverage: 100%)
Gene names: GSU3395, putA
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand EDO 22 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 95.246Å b: 151.209Å c: 175.126Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.192
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Physiological implications of arginine metabolism in plants.
Winter et al. (2015)
4 more

9 mentions without citation

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