› 2ypv

X-ray diffraction
1.8Å resolution

Crystal structure of the Meningococcal vaccine antigen factor H binding protein in complex with a bactericidal antibody

Released:
DOI: 10.2210/pdb2ypv/pdb
PDB entry 2ypv coloured by chain, front view.
PDB entry 2ypv coloured by chain, side view.
PDB entry 2ypv coloured by chain, top view.
Source organisms:
Primary publication:
Defining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigen.
Malito E, Faleri A, Lo Surdo P, Veggi D, Maruggi G, Grassi E, Cartocci E, Bertoldi I, Genovese A, Santini L, Romagnoli G, Borgogni E, Brier S, Lo Passo C, Domina M, Castellino F, Felici F, van der Veen S, Johnson S, Lea SM, Tang CM, Pizza M, Savino S, Norais N, Rappuoli R, Bottomley MJ, Masignani V
Proc Natl Acad Sci U S A 110 3304-9 (2013)
PMID: 23396847

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-212765 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Factor H binding protein Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 26.84 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9JXV4 (Residues: 23-274; Coverage: 99%)
Gene names: NMB1870, fhbP
Sequence domains:
Structure domains:
FAB 12C1 Chain: H
Molecule details ›
Chain: H
Length: 218 amino acids
Theoretical weight: 23.4 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
FAB 12C1 Chain: L
Molecule details ›
Chain: L
Length: 214 amino acids
Theoretical weight: 23.84 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand EDO 9 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 58.8Å b: 81.85Å c: 152.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.225
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

27 review citations

Hydrogen/deuterium exchange mass spectrometry for probing higher order structure of protein therapeutics: methodology and applications.
Wei et al. (2014)
26 more

13 mentions without citation

Protein Crystallography in Vaccine Research and Development.
Malito et al. (2015)
12 more