9wjk

Crystal structure of mouse EOGT-UDP complex

spinqualitylabelsall models 9wjk, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9wjk is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: EDO, NAG, UDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EOGT_MOUSE Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. Publication Abstract from PubMed Epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase (EOGT), a glycosyltransferase (GT) 61 family member, catalyzes O-N-acetylglucosamine (O-GlcNAc) transfer from uridine diphosphate (UDP)-GlcNAc to serine or threonine residues within EGF domains in the endoplasmic reticulum. In this study, we determined the crystal structure of the EOGT-UDP complex and identified the critical residues mediating their interactions, which were validated via site-directed mutagenesis and enzyme activity assays. These residues were conserved in EOGT orthologs across metazoans, and UDP binding occurred independently of divalent metal ions and the canonical Asp-X-Asp motif. Although EOGT catalyzes O-GlcNAcylation, similar to O-GlcNAc transferase (OGT), it shares little sequence similarity with OGT and belongs to a distinct GT family. Instead, EOGT is more closely related to protein O-linked-mannose beta1,4-N-acetylglucosaminyltransferase 2 (POMGNT2). Structural comparison with POMGNT2 revealed a conserved triad of one asparagine and two arginine residues, the N-R-R constellation. These elements were conserved across metazoans and green plants (Viridiplantae), suggesting a unifying mechanism of UDP recognition and providing a framework to interpret disease-associated EOGT mutations and assess the evolution of catalytically active GT61 family enzymes. Crystal structure of epidermal growth factor domain-specific O-linked N-acetylglucosamine transferase reveals a conserved N-R-R constellation for uridine diphosphate recognition in the GT61 family.,Tashima Y, Nagae M, Jiang J, Okajima T PNAS Nexus. 2026 Apr 15;5(4):pgag115. doi: 10.1093/pnasnexus/pgag115. eCollection , 2026 Apr. PMID:42058885 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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