› 5omi

X-ray diffraction
2.56Å resolution

Crystal structure of GP2 from Lassa virus in a post fusion conformation

Released:
DOI: 10.2210/pdb5omi/pdb
Model geometry
Fit model/data
PDB entry 5omi coloured by chain, front view.
PDB entry 5omi coloured by chain, side view.
PDB entry 5omi coloured by chain, top view.
Source organism: Mammarenavirus lassaense
Primary publication:
Variations in Core Packing of GP2 from Old World Mammarenaviruses in their Post-Fusion Conformations Affect Membrane-Fusion Efficiencies.
Shulman A, Katz M, Cohen-Dvashi H, Greenblatt HM, Levy Y, Diskin R
J Mol Biol 431 2095-2111 (2019)
PMID: 31004664

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoprotein G2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 118 amino acids
Theoretical weight: 13.73 KDa
Source organism: Mammarenavirus lassaense
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P08669 (Residues: 306-419; Coverage: 23%)
Gene names: GP-C, GPC

Ligands and Environments

3 bound ligands:
Ligand CL 2 x CL
Ligand NAG 3 x NAG
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 58.318Å b: 103.433Å c: 171.551Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.231 0.286
Expression system: Trichoplusia ni

Quick links

Citations

1 review citation

The underlying mechanisms of arenaviral entry through matriglycan.
Katz et al. (2024)
6 other articles

8 mentions without citation

Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure.
Hulswit et al. (2021)
7 more