Crystal structure of a virus-encoded putative glycosyltransferase

Ye Xiang, Ulrich Baxa, Ying Zhang, Alasdair C. Steven, Gentry L. Lewis, James L. Van Etten, Michael G. Rossmann

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

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-Å 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 Å.

Original languageEnglish (US)
Pages (from-to)12265-12273
Number of pages9
JournalJournal of virology
Volume84
Issue number23
DOIs
StatePublished - Dec 2010

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint Dive into the research topics of 'Crystal structure of a virus-encoded putative glycosyltransferase'. Together they form a unique fingerprint.

  • Cite this

    Xiang, Y., Baxa, U., Zhang, Y., Steven, A. C., Lewis, G. L., Van Etten, J. L., & Rossmann, M. G. (2010). Crystal structure of a virus-encoded putative glycosyltransferase. Journal of virology, 84(23), 12265-12273. https://doi.org/10.1128/JVI.01303-10