3KYC

Human SUMO E1 complex with a SUMO1-AMP mimic

3KYC の概要

• エントリーDOI: 10.2210/pdb3kyc/pdb
• 関連するPDBエントリー: 3KYD
• 分子名称: SUMO-activating enzyme subunit 1, SUMO-activating enzyme subunit 2, Small ubiquitin-related modifier 1, ... (6 entities in total)
• 機能のキーワード: e1, sumo, ubiquitin, thioester, adenylation, inhibitor, acyl-adenylate intermediate, acetylation, ligase, nucleus, phosphoprotein, ubl conjugation pathway, atp-binding, nucleotide-binding, polymorphism, cytoplasm, isopeptide bond, membrane
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus : Q9UBE0; Cytoplasm: Q9UBT2; Nucleus membrane: P63165
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 123564.07

構造登録者

Lima, C.D. (登録日: 2009-12-05, 公開日: 2010-02-16, 最終更新日: 2024-11-06)

主引用文献

Olsen, S.K.,Capili, A.D.,Lu, X.,Tan, D.S.,Lima, C.D.
Active site remodelling accompanies thioester bond formation in the SUMO E1.
Nature, 463:906-912, 2010

PubMed Abstract: E1 enzymes activate ubiquitin (Ub) and ubiquitin-like (Ubl) proteins in two steps by carboxy-terminal adenylation and thioester bond formation to a conserved catalytic cysteine in the E1 Cys domain. The structural basis for these intermediates remains unknown. Here we report crystal structures for human SUMO E1 in complex with SUMO adenylate and tetrahedral intermediate analogues at 2.45 and 2.6 A, respectively. These structures show that side chain contacts to ATP.Mg are released after adenylation to facilitate a 130 degree rotation of the Cys domain during thioester bond formation that is accompanied by remodelling of key structural elements including the helix that contains the E1 catalytic cysteine, the crossover and re-entry loops, and refolding of two helices that are required for adenylation. These changes displace side chains required for adenylation with side chains required for thioester bond formation. Mutational and biochemical analyses indicate these mechanisms are conserved in other E1s.

PubMed: 20164921
DOI: 10.1038/nature08765

実験手法

X-RAY DIFFRACTION (2.45 Å)