| http://purl.uniprot.org/citations/31831667 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31831667 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31831667 | http://www.w3.org/2000/01/rdf-schema#comment | "Oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto secretory proteins in the endoplasmic reticulum. Mammals express two distinct OST complexes that act in a cotranslational (OST-A) or posttranslocational (OST-B) manner. Here, we present high-resolution cryo-electron microscopy structures of human OST-A and OST-B. Although they have similar overall architectures, structural differences in the catalytic subunits STT3A and STT3B facilitate contacts to distinct OST subunits, DC2 in OST-A and MAGT1 in OST-B. In OST-A, interactions with TMEM258 and STT3A allow ribophorin-I to form a four-helix bundle that can bind to a translating ribosome, whereas the equivalent region is disordered in OST-B. We observed an acceptor peptide and dolichylphosphate bound to STT3B, but only dolichylphosphate in STT3A, suggesting distinct affinities of the two OST complexes for protein substrates."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.aaz3505"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.aaz3505"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/author | "Locher K.P."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/author | "Locher K.P."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/author | "Ramirez A.S."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/author | "Ramirez A.S."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/author | "Kowal J."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/author | "Kowal J."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/pages | "1372-1375"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/pages | "1372-1375"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/title | "Cryo-electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/title | "Cryo-electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B."xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/volume | "366"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://purl.uniprot.org/core/volume | "366"xsd:string |
| http://purl.uniprot.org/citations/31831667 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/31831667 |
| http://purl.uniprot.org/citations/31831667 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/31831667 |
| http://purl.uniprot.org/citations/31831667 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/31831667 |
| http://purl.uniprot.org/citations/31831667 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/31831667 |