5HKH

Crystal structure of Ufm1 in complex with UBA5

5HKH の概要

• エントリーDOI: 10.2210/pdb5hkh/pdb
• 分子名称: Ubiquitin-fold modifier 1, ASP-ASN-GLU-TRP-GLY-ILE-GLU-LEU-VAL (3 entities in total)
• 機能のキーワード: signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 19465.29

構造登録者

Huber, J.,Doetsch, V.,Rogov, V.V.,Akutsu, M. (登録日: 2016-01-14, 公開日: 2016-03-09, 最終更新日: 2024-01-10)

主引用文献

Habisov, S.,Huber, J.,Ichimura, Y.,Akutsu, M.,Rogova, N.,Loehr, F.,McEwan, D.G.,Johansen, T.,Dikic, I.,Doetsch, V.,Komatsu, M.,Rogov, V.V.,Kirkin, V.
Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation.
J.Biol.Chem., 291:9025-9041, 2016

PubMed Abstract: The covalent conjugation of ubiquitin-fold modifier 1 (UFM1) to proteins generates a signal that regulates transcription, response to cell stress, and differentiation. Ufmylation is initiated by ubiquitin-like modifier activating enzyme 5 (UBA5), which activates and transfers UFM1 to ubiquitin-fold modifier-conjugating enzyme 1 (UFC1). The details of the interaction between UFM1 and UBA5 required for UFM1 activation and its downstream transfer are however unclear. In this study, we described and characterized a combined linear LC3-interacting region/UFM1-interacting motif (LIR/UFIM) within the C terminus of UBA5. This single motif ensures that UBA5 binds both UFM1 and light chain 3/γ-aminobutyric acid receptor-associated proteins (LC3/GABARAP), two ubiquitin (Ub)-like proteins. We demonstrated that LIR/UFIM is required for the full biological activity of UBA5 and for the effective transfer of UFM1 onto UFC1 and a downstream protein substrate both in vitro and in cells. Taken together, our study provides important structural and functional insights into the interaction between UBA5 and Ub-like modifiers, improving the understanding of the biology of the ufmylation pathway.

PubMed: 26929408
DOI: 10.1074/jbc.M116.715474

実験手法

X-RAY DIFFRACTION (2.55 Å)