7MEX
Structure of yeast Ubr1 in complex with Ubc2 and N-degron
7MEX の概要
| エントリーDOI | 10.2210/pdb7mex/pdb |
| EMDBエントリー | 23806 23807 |
| 分子名称 | Ubiquitin, Ubiquitin-conjugating enzyme E2 2, N-degron, ... (5 entities in total) |
| 機能のキーワード | ubiquitin e3 ligase, ubiquitination, ubr1, ubc2, degron, n-end rule, transferase |
| 由来する生物種 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 255958.15 |
| 構造登録者 | |
| 主引用文献 | Pan, M.,Zheng, Q.,Wang, T.,Liang, L.,Mao, J.,Zuo, C.,Ding, R.,Ai, H.,Xie, Y.,Si, D.,Yu, Y.,Liu, L.,Zhao, M. Structural insights into Ubr1-mediated N-degron polyubiquitination. Nature, 600:334-338, 2021 Cited by PubMed Abstract: The N-degron pathway targets proteins that bear a destabilizing residue at the N terminus for proteasome-dependent degradation. In yeast, Ubr1-a single-subunit E3 ligase-is responsible for the Arg/N-degron pathway. How Ubr1 mediates the initiation of ubiquitination and the elongation of the ubiquitin chain in a linkage-specific manner through a single E2 ubiquitin-conjugating enzyme (Ubc2) remains unknown. Here we developed chemical strategies to mimic the reaction intermediates of the first and second ubiquitin transfer steps, and determined the cryo-electron microscopy structures of Ubr1 in complex with Ubc2, ubiquitin and two N-degron peptides, representing the initiation and elongation steps of ubiquitination. Key structural elements, including a Ubc2-binding region and an acceptor ubiquitin-binding loop on Ubr1, were identified and characterized. These structures provide mechanistic insights into the initiation and elongation of ubiquitination catalysed by Ubr1. PubMed: 34789879DOI: 10.1038/s41586-021-04097-8 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.35 Å) |
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