Structural highlights
Function
G0SG42_CHATD
Publication Abstract from PubMed
The glycoside hydrolase family 31 (GH31) alpha-glucosidases play vital roles in catabolic and regulated degradation, including the alpha-subunit of glucosidase II (GIIalpha), which catalyzes trimming of the terminal glucose residues of N-glycan in glycoprotein processing coupled with quality control in the endoplasmic reticulum. Among the known GH31 enzymes, only GIIalpha functions with its binding partner, regulatory beta-subunit (GIIbeta), which harbors a lectin domain for substrate recognition. Although the structural data have been reported for GIIalpha and the GIIbeta lectin domain, the interaction mode between GIIalpha and GIIbeta remains unknown. Here, we determined the structure of a complex formed between GIIalpha and the GIIalpha-binding domain of GIIbeta, thereby providing a structural basis underlying the functional extension of this unique GH31 enzyme. This article is protected by copyright. All rights reserved.
Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.,Satoh T, Toshimori T, Noda M, Uchiyama S, Kato K Protein Sci. 2016 Aug 31. doi: 10.1002/pro.3031. PMID:27576940[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Satoh T, Toshimori T, Noda M, Uchiyama S, Kato K. Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control. Protein Sci. 2016 Aug 31. doi: 10.1002/pro.3031. PMID:27576940 doi:http://dx.doi.org/10.1002/pro.3031
