Weak and Transient Protein Interactions Determined by Solid-State NMR.
Despite their roles in controlling many cellular processes, weak and transient interactions between large structured macromolecules and disordered protein segments cannot currently be characterized at atomic resolution by X-ray crystallography or solution NMR. Solid-state NMR does not suffer from the molecular size limitations affecting solution NMR, and it can be applied to molecules in different aggregation states, including non-crystalline precipitates and sediments. A solid-state NMR approach based on high magnetic fields, fast magic-angle sample spinning, and deuteration provides chemical-shift and relaxation mapping that enabled the characterization of the structure and dynamics of the transient association between two regions in an 80 kDa protein assembly. This led to direct verification of a mechanism of regulation of E. coli DNA metabolism.
Centre de RMN à Très Hauts Champs-, Université de Lyon, Institut de Sciences Analytiques (CNRS/ ENS-Lyon/ UCB Lyon 1), 69100, Villeurbanne, France.
Hugh R W
HR
Dannatt
Centre de RMN à Très Hauts Champs-, Université de Lyon, Institut de Sciences Analytiques (CNRS/ ENS-Lyon/ UCB Lyon 1), 69100, Villeurbanne, France.
Michele
M
Felletti
Centre de RMN à Très Hauts Champs-, Université de Lyon, Institut de Sciences Analytiques (CNRS/ ENS-Lyon/ UCB Lyon 1), 69100, Villeurbanne, France.
Stefan
S
Jehle
Centre for Medical and Molecular Bioscience, School of Chemistry, University of Wollongong, Wollongong, New South Wales, 2522, Australia.
Yao
Y
Wang
Centre de RMN à Très Hauts Champs-, Université de Lyon, Institut de Sciences Analytiques (CNRS/ ENS-Lyon/ UCB Lyon 1), 69100, Villeurbanne, France.|Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015, Lausanne, Switzerland.
Lyndon
L
Emsley
Centre for Medical and Molecular Bioscience, School of Chemistry, University of Wollongong, Wollongong, New South Wales, 2522, Australia.
Nicholas E
NE
Dixon
Centre de RMN à Très Hauts Champs-, Université de Lyon, Institut de Sciences Analytiques (CNRS/ ENS-Lyon/ UCB Lyon 1), 69100, Villeurbanne, France.
Anne
A
Lesage
Centre de RMN à Très Hauts Champs-, Université de Lyon, Institut de Sciences Analytiques (CNRS/ ENS-Lyon/ UCB Lyon 1), 69100, Villeurbanne, France. guido.pintacuda@ens-lyon.fr.
Guido
G
Pintacuda
DNA replication; magic angle spinning; protein structure; protein-protein interactions; solid-state NMR