2BA0

Archaeal exosome core

2BA0 の概要

• エントリーDOI: 10.2210/pdb2ba0/pdb
• 関連するPDBエントリー: 2BA1
• 分子名称: Archaeal exosome RNA binding protein RRP4, Archaeal exosome RNA binding protein RRP41, Archaeal exosome RNA binding protein RRP42, ... (4 entities in total)
• 機能のキーワード: exosome, rnase ph, rna degradation, exoribonuclease, rna binding, s1domain, kh domain, archaeal, rna binding protein
• 由来する生物種: Archaeoglobus fulgidus; 詳細
• 細胞内の位置: Cytoplasm : O29758 O29757 O29756
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 249467.56

構造登録者

Buttner, K.,Wenig, K.,Hopfner, K.P. (登録日: 2005-10-13, 公開日: 2005-11-22, 最終更新日: 2024-02-14)

主引用文献

Buttner, K.,Wenig, K.,Hopfner, K.P.
Structural framework for the mechanism of archaeal exosomes in RNA processing.
Mol.Cell, 20:461-471, 2005

PubMed Abstract: Exosomes emerge as central 3'-->5' RNA processing and degradation machineries in eukaryotes and archaea. We determined crystal structures of two 230 kDa nine subunit archaeal exosome isoforms. Both exosome isoforms contain a hexameric ring of RNase phosphorolytic (PH) domain subunits with a central chamber. Tungstate soaks identified three phosphorolytic active sites in this processing chamber. A trimer of Csl4 or Rrp4 subunits forms a multidomain macromolecular interaction surface on the RNase-PH domain ring with central S1 domains and peripheral KH and zinc-ribbon domains. Structural and mutational analyses suggest that the S1 domains and a subsequent neck in the RNase-PH domain ring form an RNA entry pore to the processing chamber that only allows access of unstructured RNA. This structural framework can mechanistically unify observed features of exosomes, including processive degradation of unstructured RNA, the requirement for regulatory factors to degrade structured RNA, and left-over tails in rRNA trimming.

PubMed: 16285927
DOI: 10.1016/j.molcel.2005.10.018

実験手法

X-RAY DIFFRACTION (2.7 Å)