1V92

Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97

1V92 の概要

• エントリーDOI: 10.2210/pdb1v92/pdb
• NMR情報: BMRB: 5876
• 分子名称: NSFL1 cofactor p47 (1 entity in total)
• 機能のキーワード: 3-helix bundle, recombination
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus: O35987
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5172.61

構造登録者

Yuan, X.,Simpson, P.,Mckeown, C.,Kondo, H.,Uchiyama, K.,Wallis, R.,Dreveny, I.,Keetch, C.,Zhang, X.,Robinson, C.,Freemont, P.,Matthews, S. (登録日: 2004-01-19, 公開日: 2004-04-06, 最終更新日: 2023-12-27)

主引用文献

Yuan, X.,Simpson, P.,McKeown, C.,Kondo, H.,Uchiyama, K.,Wallis, R.,Dreveny, I.,Keetch, C.,Zhang, X.,Robinson, C.,Freemont, P.,Matthews, S.
Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97
Embo J., 23:1463-1473, 2004

PubMed Abstract: 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.

PubMed: 15029246
DOI: 10.1038/sj.emboj.7600152

実験手法

SOLUTION NMR