9DQB

Cryo-EM structure of a double-loaded SUMO E1-E2-SUMO1 complex.

9DQB の概要

• エントリーDOI: 10.2210/pdb9dqb/pdb
• EMDBエントリー: 47110
• 分子名称: SUMO-conjugating enzyme UBC9, Small ubiquitin-related modifier 1, SUMO-activating enzyme subunit 1, ... (7 entities in total)
• 機能のキーワード: sumo1(a), sumo1(t), sae1, ubc9, uba2, ligase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 149179.54

構造登録者

Jia, L.,Nayak, D.,Ruben, E.A.,Nayak, A.,Wasmuth, E.V.,Olsen, S.K. (登録日: 2024-09-23, 公開日: 2025-10-01, 最終更新日: 2025-12-24)

主引用文献

Nayak, A.,Nayak, D.,Jia, L.,Ruben, E.A.,Viswanadhapalli, S.,Dos Santos Bury, P.,Nassar, K.M.,Yu, C.H.,Tumanova, A.A.,Stratton, C.M.,Ebadi, P.,Ivanov, D.N.,Sung, P.,Vadlamudi, R.K.,Wasmuth, E.V.,Olsen, S.K.
Cryo-EM structures reveal the molecular mechanism of SUMO E1-E2 thioester transfer.
Nat.Struct.Mol.Biol., 32:2441-2453, 2025

PubMed Abstract: Post-translational modification of proteins by SUMO (small ubiquitin-like modifier) regulates fundamental cellular processes and occurs through the sequential interactions and activities of three enzymes: E1, E2 and E3. SUMO E1 activates SUMO in a two-step process involving adenylation and thioester bond formation, followed by transfer of SUMO to its dedicated E2 enzyme, UBC9. This process is termed E1-E2 thioester transfer (or transthioesterification). Despite its fundamental importance, the molecular basis for SUMO E1-UBC9 thioester transfer and the molecular rules governing SUMO E1-UBC9 specificity are poorly understood. Here we present cryo-EM reconstructions of human SUMO E1 in complex with UBC9, SUMO1 adenylate and SUMO1 thioester intermediate. Our structures reveal drastic conformational changes that accompany thioester transfer, providing insights into the molecular recognition of UBC9 by SUMO E1 and delineating the rules that govern SUMO E1-UBC9 specificity. Collectively, our structural, biochemical and cell-based studies elucidate the molecular mechanisms by which SUMOylation exerts its essential biological functions.

PubMed: 40999065
DOI: 10.1038/s41594-025-01681-8

実験手法

ELECTRON MICROSCOPY (3.6 Å)