› 1yqg

X-ray diffraction
1.9Å resolution

Crystal structure of a pyrroline-5-carboxylate reductase from neisseria meningitides mc58

Released:
DOI: 10.2210/pdb1yqg/pdb
PDB entry 1yqg coloured by chain, front view.
PDB entry 1yqg coloured by chain, side view.
PDB entry 1yqg coloured by chain, top view.
Source organism: Neisseria meningitidis MC58
Primary publication:
Crystal structures of delta1-pyrroline-5-carboxylate reductase from human pathogens Neisseria meningitides and Streptococcus pyogenes.
Nocek B, Chang C, Li H, Lezondra L, Holzle D, Collart F, Joachimiak A
J Mol Biol 354 91-106 (2005)
PMID: 16233902

Function and Biology Details

Reaction catalysed: 
L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191741 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrroline-5-carboxylate reductase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.8 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9K1N1 (Residues: 1-263; Coverage: 100%)
Gene names: NMB0055, proC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21212
Unit cell:
a: 89.526Å b: 49.845Å c: 65.534Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.241
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Role of Na+ and K+ in enzyme function.
Page et al. (2006)
5 more

5 mentions without citation

Origins of coevolution between residues distant in protein 3D structures.
Anishchenko et al. (2017)
4 more