Download MendeleyStructure of the chlorovirus PBCV-1 major capsid glycoprotein determined by combining crystallographic and carbohydrate molecular modeling approaches.
De Castro, C., Klose, T., Speciale, I., Lanzetta, R., Molinaro, A., Van Etten, J.L., Rossmann, M.G.(2018) Proc Natl Acad Sci U S A 115: E44-E52
- PubMed: 29255015
- DOI: https://doi.org/10.1073/pnas.1613432115
- Primary Citation of Related Structures:
5TIP, 5TIQ - PubMed Abstract:
The glycans of the major capsid protein (Vp54) of Paramecium bursaria chlorella virus (PBCV-1) were recently described and found to be unusual. This prompted a reexamination of the previously reported Vp54 X-ray structure. A detailed description of the complete glycoprotein was achieved by combining crystallographic data with molecular modeling. The crystallographic data identified most of the monosaccharides located close to the protein backbone, but failed to detect those further from the glycosylation sites. Molecular modeling complemented this model by adding the missing monosaccharides and examined the conformational preference of the whole molecule, alone or within the crystallographic environment. Thus, combining X-ray crystallography with carbohydrate molecular modeling resulted in determining the complete glycosylated structure of a glycoprotein. In this case, it is the chlorovirus PBCV-1 major capsid protein.
Organizational Affiliation:
Department of Agricultural Sciences, University of Napoli, 80055 Portici, Italy; [email protected] [email protected] [email protected].
