4XD9

Structure of Rpf2-Rrs1 complex involved in ribosome biogenesis

4XD9 の概要

• エントリーDOI: 10.2210/pdb4xd9/pdb
• 分子名称: Ribosome biogenesis protein, putative (AFU_orthologue AFUA_8G04790), Ribosome biogenesis protein (Rrs1), putative (AFU_orthologue AFUA_7G04430) (3 entities in total)
• 機能のキーワード: complex, translation
• 由来する生物種: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122822.53

構造登録者

Asano, N.,Kato, K.,Yao, M. (登録日: 2014-12-19, 公開日: 2015-06-10, 最終更新日: 2024-03-20)

主引用文献

Asano, N.,Kato, K.,Nakamura, A.,Komoda, K.,Tanaka, I.,Yao, M.
Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis.
Nucleic Acids Res., 43:4746-4757, 2015

PubMed Abstract: Proteins Rpf2 and Rrs1 are required for 60S ribosomal subunit maturation. These proteins are necessary for the recruitment of three ribosomal components (5S ribosomal RNA [rRNA], RpL5 and RpL11) to the 90S ribosome precursor and subsequent 27SB pre-rRNA processing. Here we present the crystal structure of the Aspergillus nidulans (An) Rpf2-Rrs1 core complex. The core complex contains the tightly interlocked N-terminal domains of Rpf2 and Rrs1. The Rpf2 N-terminal domain includes a Brix domain characterized by similar N- and C-terminal architecture. The long α-helix of Rrs1 joins the C-terminal half of the Brix domain as if it were part of a single molecule. The conserved proline-rich linker connecting the N- and C-terminal domains of Rrs1 wrap around the side of Rpf2 and anchor the C-terminal domain of Rrs1 to a specific site on Rpf2. In addition, gel shift analysis revealed that the Rpf2-Rrs1 complex binds directly to 5S rRNA. Further analysis of Rpf2-Rrs1 mutants demonstrated that Saccharomyces cerevisiae Rpf2 R236 (corresponds to R238 of AnRpf2) plays a significant role in this binding. Based on these studies and previous reports, we have proposed a model for ribosomal component recruitment to the 90S ribosome precursor.

PubMed: 25855814
DOI: 10.1093/nar/gkv305

実験手法

X-RAY DIFFRACTION (2.35 Å)