2P73

crystal structure of a glycosyltransferase involved in the glycosylation of the major capsid of PBCV-1

Summary for 2P73

• Entry DOI: 10.2210/pdb2p73/pdb
• Related: 2P6W 2P72
• Descriptor: Putative glycosyltransferase (Mannosyltransferase) involved in glycosylating the PBCV-1 major capsid protein, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, pbcv-1 a64r, transferase
• Biological source: Paramecium bursaria Chlorella virus 1
• Total number of polymer chains: 1
• Total formula weight: 25621.53

Authors

Zhang, Y.,Xiang, Y.,Van Etten, J.L.,Rossmann, M.G. (deposition date: 2007-03-19, release date: 2007-08-21, Last modification date: 2024-02-21)

Primary citation

Zhang, Y.,Xiang, Y.,Van Etten, J.L.,Rossmann, M.G.
Structure and function of a chlorella virus-encoded glycosyltransferase.
Structure, 15:1031-1039, 2007

PubMed 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.

PubMed: 17850743
DOI: 10.1016/j.str.2007.07.006

Experimental method

X-RAY DIFFRACTION (2.3 Å)