2MHV

Solution Structure of Penicillium Antifungal Protein PAF

2MHV の概要

• エントリーDOI: 10.2210/pdb2mhv/pdb
• NMR情報: BMRB: 19657
• 分子名称: Antifungal protein (1 entity in total)
• 機能のキーワード: penicillium, antifungal, basic, disulfide, stable, chrysogenum, antifungal protein
• 由来する生物種: Penicillium chrysogenum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6263.10

構造登録者

Fizil, A.,Batta, G. (登録日: 2013-12-05, 公開日: 2014-12-10, 最終更新日: 2024-10-30)

主引用文献

Fizil, A.,Gaspari, Z.,Barna, T.,Marx, F.,Batta, G.
"Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Chemistry, 21:5136-5144, 2015

PubMed Abstract: Transition between conformational states in proteins is being recognized as a possible key factor of function. In support of this, hidden dynamic NMR structures were detected in several cases up to populations of a few percent. Here, we show by two- and three-state analysis of thermal unfolding, that the population of hidden states may weight 20-40 % at 298 K in a disulfide-rich protein. In addition, sensitive (15) N-CEST NMR experiments identified a low populated (0.15 %) state that was in slow exchange with the folded PAF protein. Remarkably, other techniques failed to identify the rest of the NMR "dark matter". Comparison of the temperature dependence of chemical shifts from experiments and molecular dynamics calculations suggests that hidden conformers of PAF differ in the loop and terminal regions and are most similar in the evolutionary conserved core. Our observations point to the existence of a complex conformational landscape with multiple conformational states in dynamic equilibrium, with diverse exchange rates presumably responsible for the completely hidden nature of a considerable fraction.

PubMed: 25676351
DOI: 10.1002/chem.201404879

実験手法

SOLUTION NMR