5CXB

Structure of Ytm1 bound to the C-terminal domain of Erb1 in P21 21 2 space group

5CXB の概要

• エントリーDOI: 10.2210/pdb5cxb/pdb
• 分子名称: Ribosome biogenesis protein YTM1, Ribosome biogenesis protein ERB1, 1,2-ETHANEDIOL, ... (7 entities in total)
• 機能のキーワード: ribosome assembly, wd40, beta-propeller, ubiquitin-like domain, protein binding
• 由来する生物種: Chaetomium thermophilum; 詳細
• 細胞内の位置: Nucleus, nucleolus : G0SFB5 G0SCK6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96498.19

構造登録者

Wegrecki, M.,Bravo, J. (登録日: 2015-07-28, 公開日: 2015-11-04, 最終更新日: 2024-01-10)

主引用文献

Wegrecki, M.,Rodriguez-Galan, O.,de la Cruz, J.,Bravo, J.
The structure of Erb1-Ytm1 complex reveals the functional importance of a high-affinity binding between two beta-propellers during the assembly of large ribosomal subunits in eukaryotes.
Nucleic Acids Res., 43:11017-11030, 2015

PubMed Abstract: Ribosome biogenesis is one of the most essential pathways in eukaryotes although it is still not fully characterized. Given the importance of this process in proliferating cells, it is obvious that understanding the macromolecular details of the interactions that take place between the assembly factors, ribosomal proteins and nascent pre-rRNAs is essentially required for the development of new non-genotoxic treatments for cancer. Herein, we have studied the association between the WD40-repeat domains of Erb1 and Ytm1 proteins. These are essential factors for the biogenesis of 60S ribosomal subunits in eukaryotes that form a heterotrimeric complex together with the also essential Nop7 protein. We provide the crystal structure of a dimer formed by the C-terminal part of Erb1 and Ytm1 from Chaetomium thermophilum at 2.1 Å resolution. Using a multidisciplinary approach we show that the β-propeller domains of these proteins interact in a novel manner that leads to a high-affinity binding. We prove that a point mutation within the interface of the complex impairs the interaction between the two proteins and negatively affects growth and ribosome production in yeast. Our study suggests insights into the association of the Erb1-Ytm1 dimer with pre-ribosomal particles.

PubMed: 26476442
DOI: 10.1093/nar/gkv1043

実験手法

X-RAY DIFFRACTION (2.1 Å)