5IET

Crystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome activator

5IET の概要

• エントリーDOI: 10.2210/pdb5iet/pdb
• 関連するPDBエントリー: 5IEU
• 分子名称: Bacterial proteasome activator, SULFATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: activator, apoptosis, gene regulation
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35123.98

構造登録者

Bai, L.,Hu, K.,Wang, T.,Jastrab, J.B.,Darwin, K.H.,Li, H. (登録日: 2016-02-25, 公開日: 2016-03-30, 最終更新日: 2024-10-30)

主引用文献

Bai, L.,Hu, K.,Wang, T.,Jastrab, J.B.,Darwin, K.H.,Li, H.
Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium tuberculosis.
Proc.Natl.Acad.Sci.USA, 113:E1983-E1992, 2016

PubMed Abstract: The human pathogen Mycobacterium tuberculosis (Mtb) requires a proteasome system to cause lethal infections in mice. We recently found that proteasome accessory factor E (PafE, Rv3780) activates proteolysis by the Mtb proteasome independently of adenosine triphosphate (ATP). Moreover, PafE contributes to the heat-shock response and virulence of Mtb Here, we show that PafE subunits formed four-helix bundles similar to those of the eukaryotic ATP-independent proteasome activator subunits of PA26 and PA28. However, unlike any other known proteasome activator, PafE formed dodecamers with 12-fold symmetry, which required a glycine-XXX-glycine-XXX-glycine motif that is not found in previously described activators. Intriguingly, the truncation of the PafE carboxyl-terminus resulted in the robust binding of PafE rings to native proteasome core particles and substantially increased proteasomal activity, suggesting that the extended carboxyl-terminus of this cofactor confers suboptimal binding to the proteasome core particle. Collectively, our data show that proteasomal activation is not limited to hexameric ATPases in bacteria.

PubMed: 27001842
DOI: 10.1073/pnas.1512094113

実験手法

X-RAY DIFFRACTION (2.88 Å)