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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/15102839 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15102839 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15102839 | http://www.w3.org/2000/01/rdf-schema#comment | "Three subfamilies of mammalian Class 1 processing alpha1,2-mannosidases (family 47 glycosidases) play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum (ER) and Golgi complex as well as influencing the timing and recognition for disposal of terminally unfolded proteins by ER-associated degradation. In an effort to define the structural basis for substrate recognition among Class 1 mannosidases, we have crystallized murine Golgi mannosidase IA (space group P2(1)2(1)2(1)), and the structure was solved to 1.5-A resolution by molecular replacement. The enzyme assumes an (alphaalpha)(7) barrel structure with a Ca(2+) ion coordinated at the base of the barrel similar to other Class 1 mannosidases. Critical residues within the barrel structure that coordinate the Ca(2+) ion or presumably bind and catalyze the hydrolysis of the glycone are also highly conserved. A Man(6)GlcNAc(2) oligosaccharide attached to Asn(515) in the murine enzyme was found to extend into the active site of an adjoining protein unit in the crystal lattice in a presumed enzyme-product complex. In contrast to an analogous complex previously isolated for Saccharomyces cerevisiae ER mannosidase I, the oligosaccharide in the active site of the murine Golgi enzyme assumes a different conformation to present an alternate oligosaccharide branch into the active site pocket. A comparison of the observed protein-carbohydrate interactions for the murine Golgi enzyme with the binding cleft topologies of the other family 47 glycosidases provides a framework for understanding the structural basis for substrate recognition among this class of enzymes."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m403065200"xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m403065200"xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Liu Z.-J."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Liu Z.-J."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Tempel W."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Tempel W."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Wang B.C."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Wang B.C."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Moremen K.W."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Moremen K.W."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Rose J."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Rose J."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Karaveg K."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/author | "Karaveg K."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/pages | "29774-29786"xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/pages | "29774-29786"xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/title | "Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases."xsd:string |
| http://purl.uniprot.org/citations/15102839 | http://purl.uniprot.org/core/title | "Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases."xsd:string |