2VSN
Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation
Summary for 2VSN
Entry DOI | 10.2210/pdb2vsn/pdb |
Descriptor | XCOGT, URIDINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | glycosyl transferase, n- acetylglucosamine, tpr, ogt, glcnac, o-glycosylation, transferase |
Biological source | XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS |
Total number of polymer chains | 2 |
Total formula weight | 123485.46 |
Authors | Martinez-Fleites, C.,Macauley, M.S.,He, Y.,Shen, D.,Vocadlo, D.,Davies, G.J. (deposition date: 2008-04-28, release date: 2008-06-10, Last modification date: 2024-05-08) |
Primary citation | Martinez-Fleites, C.,Macauley, M.S.,He, Y.,Shen, D.L.,Vocadlo, D.J.,Davies, G.J. Structure of an O-Glcnac Transferase Homolog Provides Insight Into Intracellular Glycosylation. Nat.Struct.Mol.Biol., 15:764-, 2008 Cited by PubMed Abstract: N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site. PubMed: 18536723DOI: 10.1038/NSMB.1443 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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