› 5edj

X-ray diffraction
2.3Å resolution

Crystal structure of the Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD

Released:
DOI: 10.2210/pdb5edj/pdb
PDB entry 5edj coloured by chain, front view.
PDB entry 5edj coloured by chain, side view.
PDB entry 5edj coloured by chain, top view.
Source organism: Neisseria meningitidis MC58
Primary publication:
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.
Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L
Sci Rep 7 40408 (2017)
PMID: 28084396

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191735 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FrpC operon protein Chain: A
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 27.03 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K129 (Residues: 29-257; Coverage: 89%)
Gene name: NMB0364
Sequence domains: RTX iron-regulated protein FrpC

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P64
Unit cell:
a: 115.39Å b: 115.39Å c: 38.812Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.183 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Biological Functions of the Secretome of Neisseria meningitidis.
Tommassen et al. (2017)
4 other articles

3 mentions without citation

The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments.
Cole et al. (2021)
2 more