3WZ0

On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis

3WZ0 の概要

• エントリーDOI: 10.2210/pdb3wz0/pdb
• 関連するPDBエントリー: 3WYZ
• 分子名称: Ribonuclease P protein component 3, Ribonuclease P protein component 2 (3 entities in total)
• 機能のキーワード: tim barrel-like structure, rrm-like structure, pre-trna cleavage, hydrolase
• 由来する生物種: Thermococcus kodakarensis KOD1; 詳細
• 細胞内の位置: Cytoplasm : Q5JH47 Q5JJ62
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78761.80

構造登録者

Suematsu, K.,Ueda, T.,Nakashima, T.,Kakuta, Y.,Kimura, M. (登録日: 2014-09-11, 公開日: 2015-09-16, 最終更新日: 2024-03-20)

主引用文献

Suematsu, K.,Ueda, T.,Nakashima, T.,Kakuta, Y.,Kimura, M.
On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis.
Biosci.Biotechnol.Biochem., 79:952-959, 2015

PubMed Abstract: The ribonuclease P (RNase P) proteins TkoPop5 and TkoRpp30, homologs of human Pop5 and Rpp30, respectively, in the hyperthermophilic archaeon Thermococcus kodakarensis were prepared and characterized with respect to pre-tRNA cleavage activity using the reconstitution system of the well-studied Pyrococcus horikoshii RNase P. The reconstituted particle containing TkoPop5 in place of the P. horikoshii counterpart PhoPop5 retained pre-tRNA cleavage activity comparable to that of the reconstituted P. horikoshii RNase P, while that containing TkoRpp30 instead of its corresponding protein PhoRpp30 had slightly lower activity than the P. horikoshii RNase P. Moreover, we determined crystal structures of TkoRpp30 alone and in complex with TkoPop5. Like their P. horikoshii counterparts, whose structures were solved previously, TkoRpp30 and TkoPop5 fold into TIM barrel and RRM-like fold, respectively. This finding demonstrates that RNase P proteins in T. kodakarensis and P. horikoshii are interchangeable and that their three-dimensional structures are highly conserved.

PubMed: 25704799
DOI: 10.1080/09168451.2014.1003130

実験手法

X-RAY DIFFRACTION (2.79 Å)