7PVN

Crystal Structure of Human UBA6 in Complex with ATP

7PVN の概要

• エントリーDOI: 10.2210/pdb7pvn/pdb
• 分子名称: Ubiquitin-like modifier-activating enzyme 6, ADENOSINE-5'-TRIPHOSPHATE, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: atp, e1 activating enzyme, fat10, ubiquitin, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 239780.39

構造登録者

Truongvan, N.,Li, S.,Schindelin, H. (登録日: 2021-10-05, 公開日: 2022-08-31, 最終更新日: 2024-11-20)

主引用文献

Truongvan, N.,Li, S.,Misra, M.,Kuhn, M.,Schindelin, H.
Structures of UBA6 explain its dual specificity for ubiquitin and FAT10.
Nat Commun, 13:4789-4789, 2022

PubMed Abstract: The covalent modification of target proteins with ubiquitin or ubiquitin-like modifiers is initiated by E1 activating enzymes, which typically transfer a single modifier onto cognate conjugating enzymes. UBA6 is an unusual E1 since it activates two highly distinct modifiers, ubiquitin and FAT10. Here, we report crystal structures of UBA6 in complex with either ATP or FAT10. In the UBA6-FAT10 complex, the C-terminal domain of FAT10 binds to where ubiquitin resides in the UBA1-ubiquitin complex, however, a switch element ensures the alternate recruitment of either modifier. Simultaneously, the N-terminal domain of FAT10 interacts with the 3-helix bundle of UBA6. Site-directed mutagenesis identifies residues permitting the selective activation of either ubiquitin or FAT10. These results pave the way for studies investigating the activation of either modifier by UBA6 in physiological and pathophysiological settings.

PubMed: 35970836
DOI: 10.1038/s41467-022-32040-6

実験手法

X-RAY DIFFRACTION (2.71 Å)