2CM0
The PUB domain functions as a p97 binding module in human peptide N-glycanase.
Summary for 2CM0
| Entry DOI | 10.2210/pdb2cm0/pdb |
| Related | 2CCQ |
| Descriptor | PEPTIDE N-GLYCANASE HOMOLOG, DI(HYDROXYETHYL)ETHER, BETA-MERCAPTOETHANOL, ... (4 entities in total) |
| Functional Keywords | transferase, kinase, pug domain |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 11099.70 |
| Authors | Allen, M.D.,Buchberger, A.,Bycroft, M. (deposition date: 2006-05-03, release date: 2006-06-28, Last modification date: 2023-12-13) |
| Primary citation | Allen, M.D.,Buchberger, A.,Bycroft, M. The Pub Domain Functions as a P97 Binding Module in Human Peptide N-Glycanase. J.Biol.Chem., 281:25502-, 2006 Cited by PubMed Abstract: The AAA ATPase p97 is a ubiquitin-selective molecular machine involved in multiple cellular processes, including protein degradation through the ubiquitin-proteasome system and homotypic membrane fusion. Specific p97 functions are mediated by a variety of cofactors, among them peptide N-glycanase, an enzyme that removes glycans from misfolded glycoproteins. Here we report the three-dimensional structure of the aminoterminal PUB domain of human peptide N-glycanase. We demonstrate that the PUB domain is a novel p97 binding module interacting with the D1 and/or D2 ATPase domains of p97 and identify an evolutionary conserved surface patch required for p97 binding. Furthermore, we show that the PUB and UBX domains do not bind to p97 in a mutually exclusive manner. Our results suggest that PUB domain-containing proteins constitute a widespread family of diverse p97 cofactors. PubMed: 16807242DOI: 10.1074/JBC.M601173200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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