› 6dnu

X-ray diffraction
2.28Å resolution

Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the oxidised form

Released:
DOI: 10.2210/pdb6dnu/pdb
PDB entry 6dnu coloured by chain, front view.
PDB entry 6dnu coloured by chain, side view.
PDB entry 6dnu coloured by chain, top view.
Source organism: Neisseria meningitidis alpha14
Primary publication:
Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.
Smith RP, Mohanty B, Mowlaboccus S, Paxman JJ, Williams ML, Headey SJ, Wang G, Subedi P, Doak BC, Kahler CM, Scanlon MJ, Heras B
J Biol Chem 293 16559-16571 (2018)
PMID: 30181210

Function and Biology Details

Reaction catalysed: 
Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111625 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein DsbD Chains: A, B
Molecule details ›
Chains: A, B
Length: 118 amino acids
Theoretical weight: 13.35 KDa
Source organism: Neisseria meningitidis alpha14
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: C6S7X6 (Residues: 499-613; Coverage: 19%)
Gene names: NMO_1340, dsbD
Sequence domains: Thioredoxin-like domain

Ligands and Environments

1 bound ligand:
Ligand P6G 6 x P6G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P41
Unit cell:
a: 35.796Å b: 35.796Å c: 188.738Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.257
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

3 citation in other articles

Structure of Arabidopsis SOQ1 lumenal region unveils C-terminal domain essential for negative regulation of photoprotective qH.
Yu et al. (2022)
2 more

1 mention without citation

Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.
Smith et al. (2018)