2cm0
From Proteopedia
Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
- | The AAA ATPase p97 is a ubiquitin-selective molecular machine involved in | + | 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. |
==About this Structure== | ==About this Structure== | ||
Line 13: | Line 13: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Allen, M | + | [[Category: Allen, M D.]] |
[[Category: Buchberger, A.]] | [[Category: Buchberger, A.]] | ||
[[Category: Bycroft, M.]] | [[Category: Bycroft, M.]] | ||
Line 22: | Line 22: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:50:03 2008'' |
Revision as of 14:50, 21 February 2008
|
THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.
Overview
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.
About this Structure
2CM0 is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The PUB domain functions as a p97 binding module in human peptide N-glycanase., Allen MD, Buchberger A, Bycroft M, J Biol Chem. 2006 Sep 1;281(35):25502-8. Epub 2006 Jun 28. PMID:16807242
Page seeded by OCA on Thu Feb 21 16:50:03 2008
Categories: Homo sapiens | Single protein | Allen, M D. | Buchberger, A. | Bycroft, M. | BME | PEG | Kinase | Pug domain | Transferase