7BFL

X-ray structure of SS-RNase-2 des116-120

7BFL の概要

• エントリーDOI: 10.2210/pdb7bfl/pdb
• 関連するPDBエントリー: 7BFK
• 分子名称: Angiogenin-1 (2 entities in total)
• 機能のキーワード: rnase, deletion mutant, salmo salar, ancient ribonuclease, hydrolase
• 由来する生物種: Salmo salar (Atlantic salmon)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 53781.60

構造登録者

Sica, F.,Russo Krauss, I.,Troisi, R. (登録日: 2021-01-04, 公開日: 2021-04-28, 最終更新日: 2024-11-20)

主引用文献

Sica, F.,Russo Krauss, I.,Troisi, R.,Bosso, A.,Culurciello, R.,Carluccio, C.,Trapani, M.,Merlino, A.,Mazzarella, L.,Pizzo, E.
The structural features of an ancient ribonuclease from Salmo salar reveal an intriguing case of auto-inhibition.
Int.J.Biol.Macromol., 182:659-668, 2021

PubMed Abstract: The superfamily of vertebrate ribonucleases, a large group of evolutionarily related proteins, continues to provide interesting structural and functional information. In particular, the crystal structure of SS-RNase-2 from Salmo salar (SS2), here presented, has revealed a novel auto-inhibition mechanism that enriches the number of inhibition strategies observed in some members of the family. Within an essentially unmodified RNase folding, the SS2 active site cleft is in part obstructed by the collapse of an extra pentapeptide inserted in the C-terminal region. This unexpected intrusion alters the organization of the catalytic triad by pushing one catalytic histidine off the pocket. Possible mechanisms to remove the active site obstruction have also been studied through the production of two mutants that provide useful information on the functionality of this intriguing version of the ribonuclease superfamily.

PubMed: 33848550
DOI: 10.1016/j.ijbiomac.2021.04.041

実験手法

X-RAY DIFFRACTION (2.88 Å)