Structural highlights
Publication Abstract from PubMed
The chloroviruses (family Phycodnaviridae), unlike most viruses, encode some, if not most, of the enzymes involved in the glycosylation of their structural proteins. Annotation of the gene product B736L from chlorovirus NY-2A suggests that it is a glycosyltransferase. The structure of the recombinantly expressed B736L protein was determined by X-ray crystallography to 2.3-A resolution, and the protein was shown to have two nucleotide-binding folds like other glycosyltransferase type B enzymes. This is the second structure of a chlorovirus-encoded glycosyltransferase and the first structure of a chlorovirus type B enzyme to be determined. B736L is a retaining enzyme and belongs to glycosyltransferase family 4. The donor substrate was identified as GDP-mannose by isothermal titration calorimetry and was shown to bind into the cleft between the two domains in the protein. The active form of the enzyme is probably a dimer in which the active centers are separated by about 40 A.
Crystal structure of a virus-encoded putative glycosyltransferase.,Xiang Y, Baxa U, Zhang Y, Steven AC, Lewis GL, Van Etten JL, Rossmann MG J Virol. 2010 Dec;84(23):12265-73. Epub 2010 Sep 22. PMID:20861263[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xiang Y, Baxa U, Zhang Y, Steven AC, Lewis GL, Van Etten JL, Rossmann MG. Crystal structure of a virus-encoded putative glycosyltransferase. J Virol. 2010 Dec;84(23):12265-73. Epub 2010 Sep 22. PMID:20861263 doi:10.1128/JVI.01303-10
