3V60

Structure of S. cerevisiae PCNA conjugated to SUMO on lysine 164

3V60 の概要

• エントリーDOI: 10.2210/pdb3v60/pdb
• 関連するPDBエントリー: 3V61 3V62
• 分子名称: Ubiquitin-like protein SMT3, Proliferating cell nuclear antigen, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ubiquitin-like protein pcna, post-translational modification dna replication dna damage response, srs2, nuclear, protein binding-dna binding protein complex, protein binding/dna binding protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus: P15873
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39168.28

構造登録者

Armstrong, A.A.,Mohideen, F.,Lima, C.D. (登録日: 2011-12-18, 公開日: 2012-02-29, 最終更新日: 2024-11-06)

主引用文献

Armstrong, A.A.,Mohideen, F.,Lima, C.D.
Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2.
Nature, 483:59-63, 2012

PubMed Abstract: Ubiquitin (Ub) and ubiquitin-like (Ubl) modifiers such as SUMO (also known as Smt3 in Saccharomyces cerevisiae) mediate signal transduction through post-translational modification of substrate proteins in pathways that control differentiation, apoptosis and the cell cycle, and responses to stress such as the DNA damage response. In yeast, the proliferating cell nuclear antigen PCNA (also known as Pol30) is modified by ubiquitin in response to DNA damage and by SUMO during S phase. Whereas Ub-PCNA can signal for recruitment of translesion DNA polymerases, SUMO-PCNA signals for recruitment of the anti-recombinogenic DNA helicase Srs2. It remains unclear how receptors such as Srs2 specifically recognize substrates after conjugation to Ub and Ubls. Here we show, through structural, biochemical and functional studies, that the Srs2 carboxy-terminal domain harbours tandem receptor motifs that interact independently with PCNA and SUMO and that both motifs are required to recognize SUMO-PCNA specifically. The mechanism presented is pertinent to understanding how other receptors specifically recognize Ub- and Ubl-modified substrates to facilitate signal transduction.

PubMed: 22382979
DOI: 10.1038/nature10883

実験手法

X-RAY DIFFRACTION (2.6 Å)