1Z5S

Crystal structure of a complex between UBC9, SUMO-1, RANGAP1 and NUP358/RANBP2

1Z5S の概要

• エントリーDOI: 10.2210/pdb1z5s/pdb
• 関連するPDBエントリー: 1KPS
• 分子名称: Ubiquitin-conjugating enzyme E2 I, Ubiquitin-like protein SMT3C, Ran GTPase-activating protein 1, ... (5 entities in total)
• 機能のキーワード: e3, ligase, sumo, ubc9, nuclear pore complex
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P63279; Nucleus membrane: P63165; Cytoplasm: P46060; Nucleus, nuclear pore complex: P49792
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 55735.83

構造登録者

Reverter, D.,Lima, C.D. (登録日: 2005-03-19, 公開日: 2005-06-07, 最終更新日: 2024-10-16)

主引用文献

Reverter, D.,Lima, C.D.
Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.
Nature, 435:687-692, 2005

PubMed Abstract: SUMO-1 (for small ubiquitin-related modifier) belongs to the ubiquitin (Ub) and ubiquitin-like (Ubl) protein family. SUMO conjugation occurs on specific lysine residues within protein targets, regulating pathways involved in differentiation, apoptosis, the cell cycle and responses to stress by altering protein function through changes in activity or cellular localization or by protecting substrates from ubiquitination. Ub/Ubl conjugation occurs in sequential steps and requires the concerted action of E2 conjugating proteins and E3 ligases. In addition to being a SUMO E3, the nucleoporin Nup358/RanBP2 localizes SUMO-conjugated RanGAP1 to the cytoplasmic face of the nuclear pore complex by means of interactions in a complex that also includes Ubc9, the SUMO E2 conjugating protein. Here we describe the 3.0-A crystal structure of a four-protein complex of Ubc9, a Nup358/RanBP2 E3 ligase domain (IR1-M) and SUMO-1 conjugated to the carboxy-terminal domain of RanGAP1. Structural insights, combined with biochemical and kinetic data obtained with additional substrates, support a model in which Nup358/RanBP2 acts as an E3 by binding both SUMO and Ubc9 to position the SUMO-E2-thioester in an optimal orientation to enhance conjugation.

PubMed: 15931224
DOI: 10.1038/nature03588

実験手法

X-RAY DIFFRACTION (3.01 Å)