6V7Q

Crystal structure of SUMO1 in complex with phosphorylated PIAS-SIM2

6V7Q の概要

• エントリーDOI: 10.2210/pdb6v7q/pdb
• 関連するPDBエントリー: 6V7P
• 分子名称: Small ubiquitin-related modifier 1, Protein PIAS (3 entities in total)
• 機能のキーワード: sumo1, pias, sumo interaction motif, peptide binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 21966.40

構造登録者

Lussier-Price, M.,Wahba, H.M.,Mascle, X.H.,Cappadocia, L.,Sakaguchi, K.,Omichinski, J.G. (登録日: 2019-12-09, 公開日: 2020-04-01, 最終更新日: 2024-10-23)

主引用文献

Lussier-Price, M.,Mascle, X.H.,Cappadocia, L.,Kamada, R.,Sakaguchi, K.,Wahba, H.M.,Omichinski, J.G.
Characterization of a C-Terminal SUMO-Interacting Motif Present in Select PIAS-Family Proteins.
Structure, 28:573-585.e5, 2020

PubMed Abstract: The human PIAS proteins are small ubiquitin-like modifier (SUMO) E3 ligases that participate in important cellular functions. Several of these functions depend on a conserved SUMO-interacting motif (SIM) located in the central region of all PIAS proteins (SIM1). Recently, it was determined that Siz2, a yeast homolog of PIAS proteins, possesses a second SIM at its C terminus (SIM2). Sequence alignment indicates that a SIM2 is also present in PIAS1-3, but not PIAS4. Using biochemical and structural studies, we demonstrate PIAS-SIM2 binds to SUMO1, but that phosphorylation of the PIAS-SIM2 or acetylation of SUMO1 alter this interaction in a manner distinct from what is observed for the PIAS-SIM1. We also show that the PIAS-SIM2 plays a key role in formation of a UBC9-PIAS1-SUMO1 complex. These results provide insights into how post-translational modifications selectively regulate the specificity of multiple SIMs found in the PIAS proteins by exploiting the plasticity built into the SUMO-SIM binding interface.

PubMed: 32348746
DOI: 10.1016/j.str.2020.04.002

実験手法

X-RAY DIFFRACTION (1.35 Å)