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Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97
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Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97
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Journal Article
Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97
2004
Overview
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 βββααβ secondary structure arrangement, where β4 pairs in a parallel fashion to β1. 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.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V
Subject
Adaptor Proteins, Signal Transducing - chemistry
/ Adaptor Proteins, Signal Transducing - genetics
/ Adaptor Proteins, Signal Transducing - metabolism
/ Adenosine Triphosphatases - chemistry
/ Adenosine Triphosphatases - genetics
/ Adenosine Triphosphatases - metabolism
/ Animals
/ EMBO31
/ EMBO40
/ Humans
/ NMR
/ Nuclear Magnetic Resonance, Biomolecular
/ Nuclear Proteins - chemistry
/ Nuclear Proteins - metabolism
/ p47
/ p97
/ Protein Structure, Quaternary
/ Protein Structure, Secondary
/ Rats
/ SEP
/ UBA
/ UBX
