3OBY

Crystal structure of Archaeoglobus fulgidus Pelota reveals inter-domain structural plasticity

3OBY の概要

• エントリーDOI: 10.2210/pdb3oby/pdb
• 関連するPDBエントリー: 3OBW
• 分子名称: Protein pelota homolog (2 entities in total)
• 機能のキーワード: sm fold, hydrolase
• 由来する生物種: Archaeoglobus fulgidus
• 細胞内の位置: Cytoplasm (Potential): O29421
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80546.11

構造登録者

Lee, H.H.,Jang, J.Y.,Yoon, H.-J.,Kim, S.J.,Suh, S.W. (登録日: 2010-08-09, 公開日: 2010-09-01, 最終更新日: 2024-03-20)

主引用文献

Lee, H.H.,Jang, J.Y.,Yoon, H.-J.,Kim, S.J.,Suh, S.W.
Crystal structures of two archaeal Pelotas reveal inter-domain structural plasticity
Biochem.Biophys.Res.Commun., 399:600-606, 2010

PubMed Abstract: Dom34 from Saccharomyces cerevisiae is one of the key players in no-go mRNA decay, a surveillance pathway by which an abnormal mRNA stalled during translation is degraded by an endonucleolytic cleavage. Its homologs called Pelota are found in other species. We showed previously that S. cerevisiae Dom34 (domain 1) has an endoribonuclease activity, which suggests its direct catalytic role in no-go decay. Pelota from Thermoplasma acidophilum and Dom34 from S. cerevisiae have been structurally characterized, revealing a tripartite architecture with a significant difference in their overall conformations. To gain further insights into structural plasticity of the Pelota proteins, we have determined the crystal structures of two archaeal Pelotas from Archaeoglobus fulgidus and Sulfolobus solfataricus. Despite the structural similarity of their individual domains to those of T. acidophilum Pelota and S. cerevisiae Dom34, their overall conformations are distinct from those of T. acidophilum Pelota and S. cerevisiae Dom34. Different overall conformations are due to conformational flexibility of the two linker regions between domains 1 and 2 and between domains 2 and 3. The observed inter-domain structural plasticity of Pelota proteins suggests that large conformational changes are essential for their functions.

PubMed: 20682285
DOI: 10.1016/j.bbrc.2010.07.121

実験手法

X-RAY DIFFRACTION (2.9 Å)