› 6h9v

X-ray diffraction
1.52Å resolution

Crystal structure of deaminated P domain from norovirus strain Saga GII-4 in complex with Fuc

Released:
DOI: 10.2210/pdb6h9v/pdb
PDB entry 6h9v coloured by chain, front view.
PDB entry 6h9v coloured by chain, side view.
PDB entry 6h9v coloured by chain, top view.
Source organism: Norovirus Hu/GII-4/Saga4/2006/JP
Primary publication:
A post-translational modification of human Norovirus capsid protein attenuates glycan binding.
Mallagaray A, Creutznacher R, D��lfer J, Mayer PHO, Grimm LL, Ordu��a JM, Trabjerg E, Stehle T, Rand KD, Blaum BS, Uetrecht C, Peters T
Nat Commun 10 1320 (2019)
PMID: 30899001

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110182 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
VP1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 34.04 KDa
Source organism: Norovirus Hu/GII-4/Saga4/2006/JP
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B5BTR7 (Residues: 225-530; Coverage: 57%)
Sequence domains: Calicivirus coat protein C-terminal
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MFU 2 x MFU
Ligand MG 2 x MG
1 modified residue:
Ligand IAS 2 x IAS

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 54.29Å b: 83.95Å c: 65.13Å
α: 90° β: 95.78° γ: 90°
R-values:
R R work R free
0.149 0.147 0.183
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Physicochemical tools for studying virus interactions with targeted cell membranes in a molecular and spatiotemporally resolved context.
Bally et al. (2021)
5 more

3 mentions without citation

Catalytic activity regulation through post-translational modification: the expanding universe of protein diversity.
Kokkinidis et al. (2020)
2 more