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

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: 18536723
DOI: 10.1038/NSMB.1443

Experimental method

X-RAY DIFFRACTION (2.75 Å)