5DFL

Crystal structure of Ube2K~Ubiquitin conjugate

5DFL の概要

• エントリーDOI: 10.2210/pdb5dfl/pdb
• 分子名称: Ubiquitin, Ubiquitin-conjugating enzyme E2 K, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: ligase, signaling protein, ligase-signaling protein complex, ligase/signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Ubiquitin: Cytoplasm : P0CG47; Cytoplasm : P61086
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31261.57

構造登録者

Middleton, A.J.,Day, C.L. (登録日: 2015-08-27, 公開日: 2015-12-02, 最終更新日: 2024-11-13)

主引用文献

Middleton, A.J.,Day, C.L.
The molecular basis of lysine 48 ubiquitin chain synthesis by Ube2K.
Sci Rep, 5:16793-16793, 2015

PubMed Abstract: The post-translational modification of proteins by ubiquitin is central to the regulation of eukaryotic cells. Substrate-bound ubiquitin chains linked by lysine 11 and 48 target proteins to the proteasome for degradation and determine protein abundance in cells, while other ubiquitin chain linkages regulate protein interactions. The specificity of chain-linkage type is usually determined by ubiquitin-conjugating enzymes (E2s). The degradative E2, Ube2K, preferentially catalyses formation of Lys48-linked chains, but like most E2s, the molecular basis for chain formation is not well understood. Here we report the crystal structure of a Ube2K~ubiquitin conjugate and demonstrate that even though it is monomeric, Ube2K can synthesize Lys48-linked ubiquitin chains. Using site-directed mutagenesis and modelling, our studies reveal a molecular understanding of the catalytic complex and identify key features required for synthesis of degradative Lys48-linked chains. The position of the acceptor ubiquitin described here is likely conserved in other E2s that catalyse Lys48-linked ubiquitin chain synthesis.

PubMed: 26592444
DOI: 10.1038/srep16793

実験手法

X-RAY DIFFRACTION (2.1 Å)