8v9q
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GALT1_MOUSE GALT1_MOUSE] Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7.<ref>PMID:9153242</ref> | [https://www.uniprot.org/uniprot/GALT1_MOUSE GALT1_MOUSE] Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7.<ref>PMID:9153242</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N-acetylgalactosaminyl-transferases (GalNAc-Ts) initiate mucin-type O-glycosylation, an abundant and complex posttranslational modification that regulates host-microbe interactions, tissue development, and metabolism. GalNAc-Ts contain a lectin domain consisting of three homologous repeats (alpha, beta, and gamma), where alpha and beta can potentially interact with O-GalNAc on substrates to enhance activity toward a nearby acceptor Thr/Ser. The ubiquitous isoenzyme GalNAc-T1 modulates heart development, immunity, and SARS-CoV-2 infectivity, but its substrates are largely unknown. Here, we show that both alpha and beta in GalNAc-T1 uniquely orchestrate the O-glycosylation of various glycopeptide substrates. The alpha repeat directs O-glycosylation to acceptor sites carboxyl-terminal to an existing GalNAc, while the beta repeat directs O-glycosylation to amino-terminal sites. In addition, GalNAc-T1 incorporates alpha and beta into various substrate binding modes to cooperatively increase the specificity toward an acceptor site located between two existing O-glycans. Our studies highlight a unique mechanism by which dual lectin repeats expand substrate specificity and provide crucial information for identifying the biological substrates of GalNAc-T1. | ||
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| + | An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.,Collette AM, Hassan SA, Schmidt SI, Lara AJ, Yang W, Samara NL Sci Adv. 2024 Mar;10(9):eadj8829. doi: 10.1126/sciadv.adj8829. Epub 2024 Feb 28. PMID:38416819<ref>PMID:38416819</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8v9q" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of mGalNAc-T1 in complex with the mucin glycopeptide Muc5AC-13, Mn2+, and UDP.
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