5ZMR

Solution Structure of the N-terminal Domain of the Yeast Rpn5

5ZMR の概要

• エントリーDOI: 10.2210/pdb5zmr/pdb
• NMR情報: BMRB: 36176
• 分子名称: 26S proteasome regulatory subunit RPN5 (1 entity in total)
• 機能のキーワード: a-helix bundle, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15618.02

構造登録者

Zhang, W.,Zhao, C.,Li, H.,Hu, Y.,Jin, C. (登録日: 2018-04-05, 公開日: 2018-09-26, 最終更新日: 2024-05-15)

主引用文献

Zhang, W.,Zhao, C.,Hu, Y.,Jin, C.
Solution structure of the N-terminal domain of proteasome lid subunit Rpn5
Biochem. Biophys. Res. Commun., 504:225-230, 2018

PubMed Abstract: The 26S proteasome is the major protein degradation machinery in living cells. The Rpn5 protein is one scaffolding subunit in the lid subcomplex of the 19S regulatory particle in the proteasome holoenzyme. Herein we report the solution structure of the N-terminal domain (NTD) of yeast Rpn5 at high resolution by NMR spectroscopy. The results show that Rpn5 NTD adopts α-solenoid-like fold in right-handed superhelical configuration formed by a number of α-helices. Structural comparisons with currently available cryo-EM structures reveal local structural differences in the first three helices between yeast and human Rpn5. The results further highlight the conformational flexibility in three possible protein interaction sites. Moreover, the structures of the NTD show large variations among different PCI-containing Rpn subunits. Our current results provide atomic-level structural basis for further investigations of protein-protein interactions and the proteasome assembly pathway.

PubMed: 30177392
DOI: 10.1016/j.bbrc.2018.08.159

実験手法

SOLUTION NMR