6H9V

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

Summary for 6H9V

• Entry DOI: 10.2210/pdb6h9v/pdb
• Related: 4OO6
• Descriptor: VP1, methyl alpha-L-fucopyranoside, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: viral capsid protein, protruding domain, viral protein, isoaspartate, isopeptide, fucose, glycan, receptor
• Biological source: Norovirus Hu/GII-4/Saga4/2006/JP
• Total number of polymer chains: 2
• Total formula weight: 68489.07

Authors

Meyer, P.H.O.,Blaum, B.S. (deposition date: 2018-08-06, release date: 2019-04-03, Last modification date: 2024-11-13)

Primary citation

Mallagaray, A.,Creutznacher, R.,Dulfer, J.,Mayer, P.H.O.,Grimm, L.L.,Orduna, J.M.,Trabjerg, E.,Stehle, T.,Rand, K.D.,Blaum, B.S.,Uetrecht, C.,Peters, T.
A post-translational modification of human Norovirus capsid protein attenuates glycan binding.
Nat Commun, 10:1320-1320, 2019

PubMed Abstract: Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains.

PubMed: 30899001
DOI: 10.1038/s41467-019-09251-5

Experimental method

X-RAY DIFFRACTION (1.52 Å)