2MSL

Solution Structure and Chemical Shift Assignments for the Apo form of the Receiver Domain of Nitrogen Regulatory Protein C (NTRC) at 35C

2MSL の概要

• エントリーDOI: 10.2210/pdb2msl/pdb
• 関連するPDBエントリー: 2MSK
• NMR情報: BMRB: 25125
• 分子名称: Nitrogen regulation protein NR(I) (1 entity in total)
• 機能のキーワード: transcription
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13636.60

構造登録者

Clarkson, M.W.,Pontiggia, F.,Villali, J.,Kern, D. (登録日: 2014-08-04, 公開日: 2015-07-01, 最終更新日: 2024-05-15)

主引用文献

Pontiggia, F.,Pachov, D.V.,Clarkson, M.W.,Villali, J.,Hagan, M.F.,Pande, V.S.,Kern, D.
Free energy landscape of activation in a signalling protein at atomic resolution.
Nat Commun, 6:7284-7284, 2015

PubMed Abstract: The interconversion between inactive and active protein states, traditionally described by two static structures, is at the heart of signalling. However, how folded states interconvert is largely unknown due to the inability to experimentally observe transition pathways. Here we explore the free energy landscape of the bacterial response regulator NtrC by combining computation and nuclear magnetic resonance, and discover unexpected features underlying efficient signalling. We find that functional states are defined purely in kinetic and not structural terms. The need of a well-defined conformer, crucial to the active state, is absent in the inactive state, which comprises a heterogeneous collection of conformers. The transition between active and inactive states occurs through multiple pathways, facilitated by a number of nonnative transient hydrogen bonds, thus lowering the transition barrier through both entropic and enthalpic contributions. These findings may represent general features for functional conformational transitions within the folded state.

PubMed: 26073309
DOI: 10.1038/ncomms8284

実験手法

SOLUTION NMR