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PDBsum entry 4n3c
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Transferase/substrate
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PDB id
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4n3c
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References listed in PDB file
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Key reference
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Title
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Hcf-1 is cleaved in the active site of o-Glcnac transferase.
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Authors
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M.B.Lazarus,
J.Jiang,
V.Kapuria,
T.Bhuiyan,
J.Janetzko,
W.F.Zandberg,
D.J.Vocadlo,
W.Herr,
S.Walker.
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Ref.
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Science, 2013,
342,
1235-1239.
[DOI no: ]
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PubMed id
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Abstract
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Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle
progression, undergoes proteolytic maturation in which any of six repeated
sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked
N-acetylglucosamine (O-GlcNAc) transferase (OGT). We report that the
tetratricopeptide-repeat domain of O-GlcNAc transferase binds the
carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage
region lies in the glycosyltransferase active site above uridine
diphosphate-GlcNAc. The conformation is similar to that of a
glycosylation-competent peptide substrate. Cleavage occurs between cysteine and
glutamate residues and results in a pyroglutamate product. Conversion of the
cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a
glycosylation substrate. Thus, protein glycosylation and HCF-1 cleavage occur in
the same active site.
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