Structure and Function of a Chlorella Virus-Encoded Glycosyltransferase

Ying Zhang, Ye Xiang, James L. Van Etten, Michael G. Rossmann

Research output: Contribution to journalArticle

17 Scopus citations


Paramecium bursaria chlorella virus-1 encodes at least five putative glycosyltransferases that are probably involved in the synthesis of the glycan components of the viral major capsid protein. The 1.6 Å crystal structure of one of these glycosyltransferases (A64R) has a mixed α/β fold containing a central, six-stranded β sheet flanked by α helices. Crystal structures of A64R, complexed with UDP, CMP, or GDP, established that only UDP bound to A64R in the presence of Mn2+, consistent with its high structural similarity to glycosyltransferases which utilize UDP as the sugar carrier. The structure of the complex of A64R, UDP-glucose, and Mn2+ showed that the largest conformational change occurred when hydrogen bonds were formed with the ligands. Unlike UDP-glucose, UDP-galactose and UDP-GlcNAc did not bind to A64R, suggesting a selective binding of UDP-glucose. Thus, UDP-glucose is most likely the sugar donor for A64R, consistent with glucose occurring in the virus major capsid protein glycans.

Original languageEnglish (US)
Pages (from-to)1031-1039
Number of pages9
Issue number9
StatePublished - Sep 11 2007



ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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