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Structure. 2007 Sep;15(9):1031-9.

Structure and function of a chlorella virus-encoded glycosyltransferase.

Author information

1
Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907, USA.

Abstract

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 A crystal structure of one of these glycosyltransferases (A64R) has a mixed alpha/beta fold containing a central, six-stranded beta sheet flanked by alpha helices. Crystal structures of A64R, complexed with UDP, CMP, or GDP, established that only UDP bound to A64R in the presence of Mn(2+), 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 Mn(2+) 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.

PMID:
17850743
PMCID:
PMC2040038
DOI:
10.1016/j.str.2007.07.006
[Indexed for MEDLINE]
Free PMC Article
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