Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation

Carlos Martinez-Fleites; Matthew S. Macauley; Yuan He; David L. Shen; David J. Vocadlo; Gideon J. Davies

doi:10.1038/nsmb.1443

Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation

Carlos Martinez-Fleites, Matthew S. Macauley, Yuan He, David L. Shen, David J. Vocadlo, Gideon J. Davies

Chemistry

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	764-765
Number of pages	2
Journal	Nature Structural & Molecular Biology
Volume	15
Issue number	7
DOIs	https://doi.org/10.1038/nsmb.1443
Publication status	Published - Jul 2008

Keywords

NUCLEOCYTOPLASMIC PROTEINS
INSULIN-RESISTANCE
DOMAIN
NUCLEAR
ALPHA

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10.1038/nsmb.1443

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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.",

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AU - Martinez-Fleites, Carlos

AU - Macauley, Matthew S.

AU - He, Yuan

AU - Shen, David L.

AU - Vocadlo, David J.

AU - Davies, Gideon J.

PY - 2008/7

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AB - 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.

KW - NUCLEOCYTOPLASMIC PROTEINS

KW - INSULIN-RESISTANCE

KW - DOMAIN

KW - NUCLEAR

KW - ALPHA

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EP - 765

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

IS - 7

ER -

Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation

Abstract

Keywords

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