5MZU

Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)

5MZU の概要

• エントリーDOI: 10.2210/pdb5mzu/pdb
• 関連するPDBエントリー: 4I2Z
• 分子名称: UNC-45 (1 entity in total)
• 機能のキーワード: chaperone, myosin folding, protein filament, ucs domain, arm repeats
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 108552.90

構造登録者

Hellerschmied, D.,Gazda, L.,Clausen, T. (登録日: 2017-02-01, 公開日: 2018-02-14, 最終更新日: 2024-11-13)

主引用文献

Hellerschmied, D.,Roessler, M.,Lehner, A.,Gazda, L.,Stejskal, K.,Imre, R.,Mechtler, K.,Dammermann, A.,Clausen, T.
UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins.
Nat Commun, 9:484-484, 2018

PubMed Abstract: Muscle development requires the coordinated activities of specific protein folding and degradation factors. UFD-2, a U-box ubiquitin ligase, has been reported to play a central role in this orchestra regulating the myosin chaperone UNC-45. Here, we apply an integrative in vitro and in vivo approach to delineate the substrate-targeting mechanism of UFD-2 and elucidate its distinct mechanistic features as an E3/E4 enzyme. Using Caenorhabditis elegans as model system, we demonstrate that UFD-2 is not regulating the protein levels of UNC-45 in muscle cells, but rather shows the characteristic properties of a bona fide E3 ligase involved in protein quality control. Our data demonstrate that UFD-2 preferentially targets unfolded protein segments. Moreover, the UNC-45 chaperone can serve as an adaptor protein of UFD-2 to poly-ubiquitinate unfolded myosin, pointing to a possible role of the UFD-2/UNC-45 pair in maintaining proteostasis in muscle cells.

PubMed: 29396393
DOI: 10.1038/s41467-018-02924-7

実験手法

X-RAY DIFFRACTION (3.8 Å)