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p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The principal role of the p97-p47 complex is in regulation of membrane fusion events. Mono-ubiquitin recognition by p47 has also been shown to be crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we describe the high-resolution solution structures of the N-terminal UBA domain and the central domain (SEP) from p47. The p47 UBA domain has the characteristic three-helix bundle fold and forms a highly stable complex with ubiquitin. We report the interaction surfaces of the two proteins and present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain adopts a novel fold with a betabetabetaalphaalphabeta secondary structure arrangement, where beta4 pairs in a parallel fashion to beta1. Based on biophysical studies, we demonstrate a clear propensity for the self-association of p47. Furthermore, p97 N binding abolishes p47 self-association, revealing the potential interaction surfaces for recognition of other domains within p97 or the substrate.

Original publication

DOI

10.1038/sj.emboj.7600152

Type

Journal article

Journal

EMBO J

Publication Date

07/04/2004

Volume

23

Pages

1463 - 1473

Keywords

Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Amino Acid Sequence, Animals, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins, Protein Folding, Protein Structure, Quaternary, Protein Structure, Secondary, Rats, Sequence Alignment, Ubiquitin