6LEY

Structure of Sil1G bound FEM1C

6LEY の概要

• エントリーDOI: 10.2210/pdb6ley/pdb
• 分子名称: Protein fem-1 homolog C,Peptide from Nucleotide exchange factor SIL1 (2 entities in total)
• 機能のキーワード: ubiquitination e3 ligase, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91230.23

構造登録者

Chen, X.,Liao, S.,Xu, C. (登録日: 2019-11-27, 公開日: 2020-10-21, 最終更新日: 2023-11-22)

主引用文献

Chen, X.,Liao, S.,Makaros, Y.,Guo, Q.,Zhu, Z.,Krizelman, R.,Dahan, K.,Tu, X.,Yao, X.,Koren, I.,Xu, C.
Molecular basis for arginine C-terminal degron recognition by Cul2 FEM1 E3 ligase.
Nat.Chem.Biol., 17:254-262, 2021

PubMed Abstract: Degrons are elements within protein substrates that mediate the interaction with specific degradation machineries to control proteolysis. Recently, a few classes of C-terminal degrons (C-degrons) that are recognized by dedicated cullin-RING ligases (CRLs) have been identified. Specifically, CRL2 using the related substrate adapters FEM1A/B/C was found to recognize C degrons ending with arginine (Arg/C-degron). Here, we uncover the molecular mechanism of Arg/C-degron recognition by solving a subset of structures of FEM1 proteins in complex with Arg/C-degron-bearing substrates. Our structural research, complemented by binding assays and global protein stability (GPS) analyses, demonstrates that FEM1A/C and FEM1B selectively target distinct classes of Arg/C-degrons. Overall, our study not only sheds light on the molecular mechanism underlying Arg/C-degron recognition for precise control of substrate turnover, but also provides valuable information for development of chemical probes for selectively regulating proteostasis.

PubMed: 33398168
DOI: 10.1038/s41589-020-00704-3

実験手法

X-RAY DIFFRACTION (2.39 Å)