› 2jsx

Solution NMR

Solution structure of the E. coli Tat proofreading chaperone protein NapD

Released:
DOI: 10.2210/pdb2jsx/pdb
PDB entry 2jsx coloured by chain, ensemble of 20 models, front view.
PDB entry 2jsx coloured by chain, ensemble of 20 models, side view.
PDB entry 2jsx coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural diversity in twin-arginine signal peptide-binding proteins.
Maillard J, Spronk CA, Buchanan G, Lyall V, Richardson DJ, Palmer T, Vuister GW, Sargent F
Proc Natl Acad Sci U S A 104 15641-6 (2007)
PMID: 17901208

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141886 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone NapD Chain: A
Molecule details ›
Chain: A
Length: 95 amino acids
Theoretical weight: 10.55 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P0A9I5 (Residues: 1-87; Coverage: 100%)
Gene names: JW2195, b2207, napD, yojF
Sequence domains: NapD protein
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli K-12

Quick links

Citations

12 review citations

The twin-arginine translocation (Tat) protein export pathway.
Palmer et al. (2012)
11 more

5 mentions without citation

Structural diversity in twin-arginine signal peptide-binding proteins.
Maillard et al. (2007)
4 more