5HGV

Structure of an O-GlcNAc transferase point mutant, D554N in complex with peptide

Summary for 5HGV

Entry DOI	10.2210/pdb5hgv/pdb
Descriptor	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET, URIDINE-5'-DIPHOSPHATE, ... (6 entities in total)
Functional Keywords	point mutant, glycosyltransferase, ogt, transferase-peptide complex, transferase/peptide
Biological source	Homo sapiens (Human) More
Total number of polymer chains	4
Total formula weight	165686.49
Authors	Janetzko, J.,Lazarus, M.B.,Walker, S. (deposition date: 2016-01-08, release date: 2016-09-14, Last modification date: 2024-10-30)
Primary citation	Janetzko, J.,Trauger, S.A.,Lazarus, M.B.,Walker, S. How the glycosyltransferase OGT catalyzes amide bond cleavage. Nat.Chem.Biol., 12:899-901, 2016 Cited by PubMed Abstract: The essential human enzyme O-linked β-N-acetylglucosamine transferase (OGT), known for modulating the functions of nuclear and cytoplasmic proteins through serine and threonine glycosylation, was unexpectedly implicated in the proteolytic maturation of the cell cycle regulator host cell factor-1 (HCF-1). Here we show that HCF-1 cleavage occurs via glycosylation of a glutamate side chain followed by on-enzyme formation of an internal pyroglutamate, which undergoes spontaneous backbone hydrolysis. PubMed: 27618188 DOI: 10.1038/nchembio.2173 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.05 Å)

Structure validation