› 6dps

X-ray diffraction
2.56Å resolution

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

Released:
DOI: 10.2210/pdb6dps/pdb
PDB entry 6dps coloured by chain, front view.
PDB entry 6dps coloured by chain, side view.
PDB entry 6dps 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

Assemblies composition:
monomeric (preferred)
homo octadecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-111625 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein DsbD Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 126 amino acids
Theoretical weight: 13.92 KDa
Source organism: Neisseria meningitidis alpha14
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: C6S7X6 (Residues: 35-158; Coverage: 20%)
Gene names: NMO_1340, dsbD
Sequence domains: Thiol:disulfide interchange protein DsbD, N-terminal
Structure domains: Thiol:disulfide interchange protein DsbD, N-terminal domain

Ligands and Environments

1 bound ligand:
Ligand ZN 32 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P213
Unit cell:
a: 147.643Å b: 147.643Å c: 147.643Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.178 0.235
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

2 citation in other articles

The Scs disulfide reductase system cooperates with the metallochaperone CueP in Salmonella copper resistance.
Subedi et al. (2019)
1 more

2 mentions without citation

Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.
Stelzl et al. (2020)
1 more