期刊
FEBS LETTERS
卷 583, 期 19, 页码 3151-3157出版社
WILEY
DOI: 10.1016/j.febslet.2009.09.020
关键词
Prokaryotic ubiquitin-like protein; Mpa; ARC; Proteasome; NMR; Mycobacterium tuberculosis
资金
- Swiss National Science Foundation (SNF)
- National Center for Excellence in Research (NCCR) Structural Biology program of the SNF
- ETH
- Fonds der Chemischen Industrie
The mycobacterial ubiquitin-like protein Pup is coupled to proteins, thereby rendering them as substrates for proteasome-mediated degradation. The Pup-tagged proteins are recruited by the proteasomal ATPase Mpa (also called ARC). Using a combination of biochemical and NMR methods, we characterize the structural determinants of Pup and its interaction with Mpa, demonstrating that Pup adopts a range of extended conformations with a short helical stretch in its C-terminal portion. We show that the N-terminal coiled-coil domain of Mpa makes extensive contacts along the central region of Pup leaving its N-terminus unconstrained and available for other functional interactions. Structured summary: MINT-7262427:pup (uniprotkb:B6DAC1) binds (MI:0407) to mpa (uniprotkb:Q0G9Y7) by pull down (MI:0096) MINT-7262440:mpa (uniprotkb:Q0G9Y7) and pup (uniprotkb:B6DAC1) bind (MI:0407) by isothermal titration calorimetry (MI:0065) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据