Nucleotide Binding Modes in a Motor Protein Revealed by 31 P- and 1 H-Detected MAS Solid-State NMR Spectroscopy.
Chembiochem
; 21(3): 324-330, 2020 02 03.
Article
en En
| MEDLINE
| ID: mdl-31310428
ABSTRACT
Protein-nucleic acid interactions play important roles not only in energy-providing reactions, such as ATP hydrolysis, but also in reading, extending, packaging, or repairing genomes. Although they can often be analyzed in detail with X-ray crystallography, complementary methods are needed to visualize them in complexes, which are not crystalline. Here, we show how solid-state NMR spectroscopy can detect and classify protein-nucleic interactions through site-specific 1 H- and 31 P-detected spectroscopic methods. The sensitivity of 1 H chemical-shift values on noncovalent interactions involved in these molecular recognition processes is exploited allowing us to probe directly the chemical bonding state, an information, which is not directly accessible from an X-ray structure. We show that these methods can characterize interactions in easy-to-prepare sediments of the 708â
kDa dodecameric DnaB helicase in complex with ADPAlF4-DNA, and this despite the very challenging size of the complex.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Resonancia Magnética Nuclear Biomolecular
/
AdnB Helicasas
/
Nucleótidos
Idioma:
En
Año:
2020
Tipo del documento:
Article