2ASQ

Solution Structure of SUMO-1 in Complex with a SUMO-binding Motif (SBM)

2ASQ の概要

• エントリーDOI: 10.2210/pdb2asq/pdb
• 関連するPDBエントリー: 1WYW 1Z5S
• 分子名称: Small ubiquitin-related modifier 1, Protein inhibitor of activated STAT2 (2 entities in total)
• 機能のキーワード: protein-peptide complex, sumo-1, small ubiquitin-like modifier 1, sumo-binding motif, sbm, protein inhibitor of activated stat, piasx, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus membrane: P63165; Nucleus speckle: O75928
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13984.62

構造登録者

Song, J.,Zhang, Z.,Hu, W.,Chen, Y. (登録日: 2005-08-23, 公開日: 2005-10-11, 最終更新日: 2024-05-22)

主引用文献

Song, J.,Zhang, Z.,Hu, W.,Chen, Y.
Small Ubiquitin-like Modifier (SUMO) Recognition of a SUMO Binding Motif: A reversal of the bound orientation
J.Biol.Chem., 280:40122-40129, 2005

PubMed Abstract: Sumoylation has recently been identified as an important mechanism that regulates protein interactions and localization in essential cellular functions, such as gene transcription, subnuclear structure formation, viral infection, and cell cycle progression. A SUMO binding amino acid sequence motif (SBM), which recognizes the SUMO moiety of modified proteins in sumoylation-dependent cellular functions, has been consistently identified by several recent studies. To understand the mechanism of SUMO recognition by the SBM, we have solved the solution structure of SUMO-1 in complex with a peptide containing the SBM derived from the protein PIASX (KVDVIDLTIESSSDEEEDPPAKR). Surprisingly, the structure reveals that the bound orientation of the SBM can reverse depending on the sequence context. The structure also reveals a novel mechanism of recognizing target sequences by a ubiquitin-like module. Unlike ubiquitin binding motifs, which all form helices and bind to the main beta-sheet of ubiquitin, the SBM forms an extended structure that binds between the alpha-helix and a beta-strand of SUMO-1. This study provides a clear mechanism of the SBM sequence variations and its recognition of the SUMO moiety in sumoylated proteins.

PubMed: 16204249
DOI: 10.1074/jbc.M507059200

実験手法

SOLUTION NMR