7PVM

NMR structure of the C. thermophilum Xrn2 zinc finger

7PVM の概要

• エントリーDOI: 10.2210/pdb7pvm/pdb
• 関連するPDBエントリー: 7OPK
• NMR情報: BMRB: 50997
• 分子名称: 5'-3' exoribonuclease, ZINC ION (2 entities in total)
• 機能のキーワード: zinc finger, rna binding protein
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3376.22

構造登録者

Overbeck, J.H.,Sprangers, R.,Wurm, J.P. (登録日: 2021-10-05, 公開日: 2022-07-06, 最終更新日: 2024-06-19)

主引用文献

Overbeck, J.H.,Stelzig, D.,Fuchs, A.L.,Wurm, J.P.,Sprangers, R.
Observation of conformational changes that underlie the catalytic cycle of Xrn2.
Nat.Chem.Biol., 18:1152-1160, 2022

PubMed Abstract: Nuclear magnetic resonance (NMR) methods that quantitatively probe motions on molecular and atomic levels have propelled the understanding of biomolecular processes for which static structures cannot provide a satisfactory description. In this work, we studied the structure and dynamics of the essential 100-kDa eukaryotic 5'→3' exoribonuclease Xrn2. A combination of complementary fluorine and methyl-TROSY NMR spectroscopy reveals that the apo enzyme is highly dynamic around the catalytic center. These observed dynamics are in agreement with a transition of the enzyme from the ground state into a catalytically competent state. We show that the conformational equilibrium in Xrn2 shifts substantially toward the active state in the presence of substrate and magnesium. Finally, our data reveal that the dynamics in Xrn2 correlate with the RNA degradation rate, as a mutation that attenuates motions also affects catalytic activity. In that light, our results stress the importance of studies that go beyond static structural information.

PubMed: 36008487
DOI: 10.1038/s41589-022-01111-6

実験手法

SOLUTION NMR