Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.
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.
Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5YW, UK.
Carlos
C
Martinez-Fleites
Matthew S
MS
Macauley
Yuan
Y
He
David L
DL
Shen
David J
DJ
Vocadlo
Gideon J
GJ
Davies
D001665:Binding Sites; D006031:Glycosylation; D006801:Humans; D042541:Intracellular Space / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D050505:Mutant Proteins / Q000378:metabolism; D017351:N-Acetylglucosaminyltransferases / Q000737:chemistry*; D040681:Structural Homology, Protein; D013329:Structure-Activity Relationship; D014974:Xanthomonas / Q000201:enzymology*
D050505:Mutant Proteins; D017351:N-Acetylglucosaminyltransferases; C063057:UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase