ArticleProceedings of the National Academy of Sciences of the United States of America2005
Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 58 citations in OpenAlex.
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation.Nutrients · 2022Review
- Loss of N-Glycanase 1 Alters Transcriptional and Translational Regulation in K562 Cell Lines.G3 (Bethesda, Md.) · 2020Article
- HR23B pathology preferentially co-localizes with p62, pTDP-43 and poly-GA in C9ORF72-linked frontotemporal dementia and amyotrophic lateral sclerosis.Acta neuropathologica communications · 2019Article
- Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog.Scientific reports · 2016Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- Article
- Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation.Scientific reports · 2015Article
- Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain.The Journal of biological chemistry · 2014Article
- Structure of the catalytic domain of the Salmonella virulence factor SseI.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum.BMC biochemistry · 2012Article
- Protein quality control in the ER: balancing the ubiquitin checkbook.Trends in cell biology · 2012Review
- Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster.PloS one · 2010Article
- The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity.The Journal of biological chemistry · 2010Article
- N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity.PloS one · 2009Article
- Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase.Glycobiology · 2009Article
- Systematic synthesis and inhibitory activity of haloacetamidyl oligosaccharide derivatives toward cytoplasmic peptide:N-glycanase.Glycoconjugate journal · 2009Article
- Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein.Biochemistry · 2006Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, misfolded proteins must be distinguished from correctly folded proteins during folding and transport processes by quality control systems. Yeast peptide:N-glycanase (yPNGase) specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists proteasome-mediated glycoprotein degradation by forming a complex with 26S proteasome through DNA repair protein, yRad23. Here, we describe the crystal structures of a yPNGase and XPC-binding domain of yRad23 (yRad23XBD, residues 238-309) complex and of a yPNGase-yRad23XBD complex bound to a caspase inhibitor, Z-VAD-fmk. yPNGase is formed with three domains, a core domain containing a Cys-His-Asp triad, a Zn-binding domain, and a Rad23-binding domain. Both N- and C-terminal helices of yPNGase interact with yRad23 through extensive hydrophobic interactions. The active site of yPNGase is located in a deep cleft that is formed with residues conserved in all PNGase members, and three sugar molecules are bound to this cleft. Complex structures in conjunction with mutational analyses revealed that the walls of the cleft block access to the active site of yPNGase by native glycoprotein, whereas the cleft is sufficiently wide to accommodate denatured glycoprotein, thus explaining the specificity of PNGase for denatured substrates.
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