› 5fgn

X-ray diffraction
2.75Å resolution

Integral membrane protein lipooligosaccharide phosphoethanolamine transferase A (EptA) from Neisseria meningitidis

Released:
DOI: 10.2210/pdb5fgn/pdb
PDB entry 5fgn coloured by chain, front view.
PDB entry 5fgn coloured by chain, side view.
PDB entry 5fgn coloured by chain, top view.
Source organism: Neisseria meningitidis serogroup B
Primary publication:
Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding.
Anandan A, Evans GL, Condic-Jurkic K, O'Mara ML, John CM, Phillips NJ, Jarvis GA, Wills SS, Stubbs KA, Moraes I, Kahler CM, Vrielink A
Proc Natl Acad Sci U S A 114 2218-2223 (2017)
PMID: 28193899

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-181484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
YhbX/YhjW/YijP/YjdB family protein Chain: A
Molecule details ›
Chain: A
Length: 550 amino acids
Theoretical weight: 62.29 KDa
Source organism: Neisseria meningitidis serogroup B
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7DD94 (Residues: 1-544; Coverage: 100%)
Gene name: NMB1638
Sequence domains:
Structure domains: Alkaline Phosphatase, subunit A

Ligands and Environments

3 bound ligands:
Ligand BGL 1 x BGL
Ligand LMT 1 x LMT
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I422
Unit cell:
a: 187.285Å b: 187.285Å c: 205.125Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.241
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Pushing the envelope: LPS modifications and their consequences.
Simpson et al. (2019)
10 more

28 mentions without citation

Anti-Virulence Therapeutic Approaches for Neisseria gonorrhoeae.
Lim et al. (2021)
27 more