2i74
From Proteopedia
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Crystal structure of mouse Peptide N-Glycanase C-terminal domain in complex with mannopentaose
Overview
The inability of certain N-linked glycoproteins to adopt their native, conformation in the endoplasmic reticulum (ER) leads to their, retrotranslocation into the cytosol and subsequent degradation by the, proteasome. In this pathway the cytosolic peptide-N-glycanase (PNGase), cleaves the N-linked glycan chains off denatured glycoproteins. PNGase is, highly conserved in eukaryotes and plays an important role in, ER-associated protein degradation. In higher eukaryotes, PNGase has an, N-terminal and a C-terminal extension in addition to its central catalytic, domain, which is structurally and functionally related to, transglutaminases. Although the N-terminal domain of PNGase is involved in, protein-protein interactions, the function of the C-terminal domain has, not previously been characterized. Here, we describe biophysical, biochemical, and crystallographic studies of the mouse PNGase C-terminal, domain, including visualization of a complex between this domain and, mannopentaose. These studies demonstrate that the C-terminal domain binds, to the mannose moieties of N-linked oligosaccharide chains, and we further, show that it enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan, chains of misfolded glycoproteins.
About this Structure
2I74 is a Single protein structure of sequence from Mus musculus with ACT and GOL as ligands. Active as Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase, with EC number 3.5.1.52 Full crystallographic information is available from OCA.
Reference
Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module., Zhou X, Zhao G, Truglio JJ, Wang L, Li G, Lennarz WJ, Schindelin H, Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17214-9. Epub 2006 Nov 6. PMID:17088551
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