Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3OY2

Crystal structure of a putative glycosyltransferase from Paramecium bursaria Chlorella virus NY2A

Summary for 3OY2
Entry DOI10.2210/pdb3oy2/pdb
Related3OY7
DescriptorGlycosyltransferase B736L (2 entities in total)
Functional Keywordsrossmann fold, glycosyltransferase, gdp-mannose, sugar, virus capsid proteins, viral protein, transferase
Biological sourceParamecium bursaria Chlorella virus NY2A (PBCV-NY2A)
Total number of polymer chains2
Total formula weight93358.59
Authors
Xiang, Y.,Rossmann, M.G. (deposition date: 2010-09-22, release date: 2010-11-17, Last modification date: 2024-02-21)
Primary citationXiang, Y.,Baxa, U.,Zhang, Y.,Steven, A.C.,Lewis, G.L.,Van Etten, J.L.,Rossmann, M.G.
Crystal structure of a virus-encoded putative glycosyltransferase
J.Virol., 84:12265-12273, 2010
Cited by
PubMed 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.
PubMed: 20861263
DOI: 10.1128/JVI.01303-10
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.31 Å)
Structure validation

237992

数据于2025-06-25公开中

PDB statisticsPDBj update infoContact PDBjnumon