› 1eq7

X-ray diffraction
1.9Å resolution

CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1eq7/pdb
PDB entry 1eq7 coloured by chain, front view.
PDB entry 1eq7 coloured by chain, side view.
PDB entry 1eq7 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution.
Shu W, Liu J, Ji H, Lu M
J Mol Biol 299 1101-12 (2000)
PMID: 10843861

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major outer membrane lipoprotein Lpp Chain: A
Molecule details ›
Chain: A
Length: 56 amino acids
Theoretical weight: 6.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69776 (Residues: 22-77; Coverage: 97%)
Gene names: JW1667, b1677, lpp, mlpA, mulI
Sequence domains: Lipoprotein leucine-zipper
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R32
Unit cell:
a: 34.363Å b: 34.363Å c: 194.135Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.214 0.269
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials.
Apostolovic et al. (2010)
15 more

9 mentions without citation

Cellular solid-state nuclear magnetic resonance spectroscopy.
Renault et al. (2012)
8 more