The PUB domain functions as a p97 binding module in human peptide N-glycanase.

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.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Nuclear Proteins, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Ubiquitin
J. Biol. Chem.
Date: Sep. 01, 2006
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