› 2z4i

X-ray diffraction
2.6Å resolution

Crystal structure of the Cpx pathway activator NlpE from Escherichia coli

Released:
DOI: 10.2210/pdb2z4i/pdb
PDB entry 2z4i coloured by chain, front view.
PDB entry 2z4i coloured by chain, side view.
PDB entry 2z4i coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli.
Hirano Y, Hossain MM, Takeda K, Tokuda H, Miki K
Structure 15 963-76 (2007)
PMID: 17698001

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoprotein NlpE Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.15 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P40710 (Residues: 21-236; Coverage: 100%)
Gene names: JW0188, b0192, cutF, nlpE
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand P6G 1 x P6G
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 22 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P43212
Unit cell:
a: 121.422Å b: 121.422Å c: 84.456Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.27
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Just scratching the surface: an expanding view of the Cpx envelope stress response.
Vogt et al. (2012)
10 more

3 mentions without citation

Insights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analyses.
Brautigam et al. (2015)
2 more