Journal
STRUCTURE
Volume 15, Issue 9, Pages 1031-1039Publisher
CELL PRESS
DOI: 10.1016/j.str.2007.07.006
Keywords
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Funding
- NCRR NIH HHS [P20 RR 15635, P20 RR015635] Funding Source: Medline
- NIAID NIH HHS [AI 11219, R37 AI011219, R37 AI011219-35, R01 AI011219] Funding Source: Medline
- NIGMS NIH HHS [GM 32441, R01 GM032441, R01 GM032441-24] Funding Source: Medline
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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 angstrom 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 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.
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