› 1kfn

X-ray diffraction
1.65Å resolution

Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants

Released:
DOI: 10.2210/pdb1kfn/pdb
PDB entry 1kfn coloured by chain, front view.
PDB entry 1kfn coloured by chain, side view.
PDB entry 1kfn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants.
Liu J, Cao W, Lu M
J Mol Biol 318 877-88 (2002)
PMID: 12054830

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 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: NSLS BEAMLINE X25
Spacegroup: R3
Unit cell:
a: 36.29Å b: 36.29Å c: 83.473Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.244 0.272
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Communication across the bacterial cell envelope depends on the size of the periplasm.
Asmar et al. (2017)
9 more

1 mention without citation

Insights on the structure and stability of Licanantase: a trimeric acid-stable coiled-coil lipoprotein from Acidithiobacillus thiooxidans.
Abarca et al. (2014)