2MHV

Solution Structure of Penicillium Antifungal Protein PAF

Summary for 2MHV

• Entry DOI: 10.2210/pdb2mhv/pdb
• NMR Information: BMRB: 19657
• Descriptor: Antifungal protein (1 entity in total)
• Functional Keywords: penicillium, antifungal, basic, disulfide, stable, chrysogenum, antifungal protein
• Biological source: Penicillium chrysogenum
• Total number of polymer chains: 1
• Total formula weight: 6263.10

Authors

Fizil, A.,Batta, G. (deposition date: 2013-12-05, release date: 2014-12-10, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

SOLUTION NMR