4JG4

Ligand concentration regulates the pathways of coupled protein folding and binding

4JG4 の概要

• エントリーDOI: 10.2210/pdb4jg4/pdb
• 分子名称: Ribonuclease P protein component, PYROPHOSPHATE (3 entities in total)
• 機能のキーワード: rna-binding, endonuclease, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14675.44

構造登録者

Tonthat, N.K. (登録日: 2013-02-28, 公開日: 2014-01-22, 最終更新日: 2024-02-28)

主引用文献

Daniels, K.G.,Tonthat, N.K.,McClure, D.R.,Chang, Y.C.,Liu, X.,Schumacher, M.A.,Fierke, C.A.,Schmidler, S.C.,Oas, T.G.
Ligand concentration regulates the pathways of coupled protein folding and binding.
J.Am.Chem.Soc., 136:822-825, 2014

PubMed Abstract: Coupled ligand binding and conformational change plays a central role in biological regulation. Ligands often regulate protein function by modulating conformational dynamics, yet the order in which binding and conformational change occurs are often hotly debated. Here we show that the "conformational selection versus induced fit" distinction on which this debate is based is a false dichotomy because the mechanism depends on ligand concentration. Using the binding of pyrophosphate (PPi) to Bacillus subtilis RNase P protein as a model, we show that coupled reactions are best understood as a change in flux between competing pathways with distinct orders of binding and conformational change. The degree of partitioning through each pathway depends strongly on PPi concentration, with ligand binding redistributing the conformational ensemble toward the folded state by both increasing folding rates and decreasing unfolding rates. These results indicate that ligand binding induces marked and varied changes in protein conformational dynamics, and that the order of binding and conformational change is ligand concentration dependent.

PubMed: 24364358
DOI: 10.1021/ja4086726

実験手法

X-RAY DIFFRACTION (2.296 Å)