6DEI

Structure of Dse3-Csm1 complex

6DEI の概要

• エントリーDOI: 10.2210/pdb6dei/pdb
• 分子名称: Monopolin complex subunit CSM1, Protein DSE3, TRIETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: monopolin, daughter cell-specific protein, protein binding-cell cycle complex, protein binding/cell cycle
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 31752.56

構造登録者

Singh, N.,Corbett, K.D. (登録日: 2018-05-12, 公開日: 2018-10-03, 最終更新日: 2023-10-11)

主引用文献

Singh, N.,Corbett, K.D.
The budding-yeast RWD protein Csm1 scaffolds diverse protein complexes through a conserved structural mechanism.
Protein Sci., 27:2094-2100, 2018

PubMed Abstract: RWD domains mediate protein-protein interactions in a variety of pathways in eukaryotes. In budding yeast, the RWD domain protein Csm1 is particularly versatile, assembling key complexes in the nucleolus and at meiotic kinetochores through multiple protein interaction surfaces. Here, we reveal a third functional context for Csm1 by identifying a new Csm1-interacting protein, Dse3. We show that Dse3 interacts with Csm1 in a structurally equivalent manner to its known binding partners Mam1 and Ulp2, despite these three proteins' lack of overall sequence homology. We theorize that the unique "clamp" structure of Csm1 and the loose sequence requirements for Csm1 binding have led to its incorporation into at least three different structural/signaling pathways in budding yeast.

PubMed: 30252178
DOI: 10.1002/pro.3515

実験手法

X-RAY DIFFRACTION (1.699 Å)