Results for “VP4” | Engineering Papers

DOE OSTI2020

Materials Data on VP4 by Materials Project

VP4 is Sylvanite-derived structured and crystallizes in the monoclinic C2/c space group. The structure is three-dimensional. V4+ is bonded to six P1- atoms to form edge-sharing VP6 octahedra. There are a spread of V–P bond distances ranging from 2.35–2.42 Å. There are two inequivalent P1- sites. In the first P1- site, P1- is bonded in a 4-coordinate geometry to one V4+ and three P1- atoms. There are two shorter (2.23 Å) and one longer (2.25 Å) P–P bond lengths. In the second P1- site, P1- is bonded in a 4-coordinate geometry to two equivalent V4+ and two P1- atoms. The P–P bond length is 2.22 Å.

36 MATERIALS SCIENCE↗

DOE OSTI2022

Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography

The VP8* domain of spike protein VP4 in group A and C rotaviruses, which cause epidemic gastroenteritis in children, exhibits a conserved galectin-like fold for recognizing glycans during cell entry. In group B rotavirus, which causes significant diarrheal outbreaks in adults, the VP8* domain (VP8*B) surprisingly lacks sequence similarity with VP8* of group A or group C rotavirus. Here, by using the recently developed AlphaFold2 for ab initio structure prediction and validating the predicted model by determining a 1.3-Å crystal structure, we show that VP8*B exhibits a novel fold distinct from the galectin fold. This fold with a β-sheet clasping an α-helix represents a new fold for glycan recognition based on glycan array screening, which shows that VP8*B recognizes glycans containing N-acetyllactosamine moiety. Although uncommon, our study illustrates how evolution can incorporate structurally distinct folds with similar functionality in a homologous protein within the same virus genus.

59 BASIC BIOLOGICAL SCIENCES↗