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http://purl.uniprot.org/citations/15713668http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15713668http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15713668http://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/15713668http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m500119200"xsd:string
http://purl.uniprot.org/citations/15713668http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m500119200"xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Tempel W."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Tempel W."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Wang B.C."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Wang B.C."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Liu Z.J."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Liu Z.J."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Moremen K.W."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Moremen K.W."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Karaveg K."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Karaveg K."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Glushka J."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Glushka J."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Siriwardena A."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/author"Siriwardena A."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/pages"16197-16207"xsd:string
http://purl.uniprot.org/citations/15713668http://purl.uniprot.org/core/pages"16197-16207"xsd:string