| http://purl.uniprot.org/citations/15486088 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15486088 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15486088 | http://www.w3.org/2000/01/rdf-schema#comment | "UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (ppGaNTases) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr). ppGaNTases are unique among glycosyltransferases in containing a C-terminal lectin domain. We present the x-ray crystal structure of a ppGaNTase, murine ppGaNTase-T1, and show that it folds to form distinct catalytic and lectin domains. The association of the two domains forms a large cleft in the surface of the enzyme that contains a Mn2+ ion complexed by invariant D209 and H211 of the "DXH" motif and by invariant H344. Each of the three potential lectin domain carbohydrate-binding sites (alpha, beta, and gamma) is located on the active-site face of the enzyme, suggesting a mechanism by which the transferase may accommodate multiple conformations of glycosylated acceptor substrates. A model of a mucin 1 glycopeptide substrate bound to the enzyme shows that the spatial separation between the lectin alpha site and a modeled active site UDP-GalNAc is consistent with the in vitro pattern of glycosylation observed for this peptide catalyzed by ppGaNTase-T1. The structure also provides a template for the larger ppGaNTase family, and homology models of several ppGaNTase isoforms predict dramatically different surface chemistries consistent with isoform-selective acceptor substrate recognition."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0405657101"xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0405657101"xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Shiloach J."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Shiloach J."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Hurley J.H."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Hurley J.H."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Tabak L.A."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Tabak L.A."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Trinh L.B."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Trinh L.B."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Fritz T.A."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/author | "Fritz T.A."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/pages | "15307-15312"xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/pages | "15307-15312"xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/title | "The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/title | "The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1."xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/volume | "101"xsd:string |
| http://purl.uniprot.org/citations/15486088 | http://purl.uniprot.org/core/volume | "101"xsd:string |