http://purl.uniprot.org/citations/15713668 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15713668 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15713668 | http://www.w3.org/2000/01/rdf-schema#comment | "Quality control in the endoplasmic reticulum (ER) determines the fate of newly synthesized glycoproteins toward either correct folding or disposal by ER-associated degradation. Initiation of the disposal process involves selective trimming of N-glycans attached to misfolded glycoproteins by ER alpha-mannosidase I and subsequent recognition by the ER degradation-enhancing alpha-mannosidase-like protein family of lectins, both members of glycosylhydrolase family 47. The unusual inverting hydrolytic mechanism catalyzed by members of this family is investigated here by a combination of kinetic and binding analyses of wild type and mutant forms of human ER alpha-mannosidase I as well as by structural analysis of a co-complex with an uncleaved thiodisaccharide substrate analog. These data reveal the roles of potential catalytic acid and base residues and the identification of a novel (3)S(1) sugar conformation for the bound substrate analog. The co-crystal structure described here, in combination with the (1)C(4) conformation of a previously identified co-complex with the glycone mimic, 1-deoxymannojirimycin, indicates that glycoside bond cleavage proceeds through a least motion conformational twist of a properly predisposed substrate in the -1 subsite. A novel (3)H(4) conformation is proposed as the exploded transition state."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m500119200"xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m500119200"xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Tempel W."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Tempel W."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Wang B.C."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Wang B.C."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Liu Z.J."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Liu Z.J."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Moremen K.W."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Moremen K.W."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Karaveg K."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Karaveg K."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Glushka J."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Glushka J."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Siriwardena A."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/author | "Siriwardena A."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/pages | "16197-16207"xsd:string |
http://purl.uniprot.org/citations/15713668 | http://purl.uniprot.org/core/pages | "16197-16207"xsd:string |