| Autor: |
Yuan, Xuemei, Simpson, Peter, Mckeown, Ciaran, Kondo, Hisao, Uchiyama, Keiji, Wallis, Russell, Dreveny, Ingrid, Keetch, Catherine, Zhang, Xiaodong, Robinson, Carol, Freemont, Paul, Matthews, Stephen |
| Předmět: |
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| Zdroj: |
EMBO Journal; 4/7/2004, Vol. 23 Issue 7, p1463-1473, 11p |
| Abstrakt: |
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 ßßßaaß secondary structure arrangement, where ß4 pairs in a parallel fashion to ß1. 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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