期刊
CHEMBIOCHEM
卷 21, 期 3, 页码 324-330出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201900439
关键词
DnaB helicases; fast MAS; hydrogen bonds; nucleotide binding; solid-state NMR spectroscopy
资金
- Swiss National Science Foundation [200020_ 159707, 200020_ 178792]
- French ANR [ANR-14-CE09-0024B]
- LABEX ECOFECT within the Universitde Lyon program Investissements d'Avenir [ANR-11-LABX-0048, ANR-11-IDEX-0007]
- ETH [SEED-69 16-1]
- European Research Council (ERC) under the European Union [741863]
- ETH Research Grant [ETH-43 17-2]
- Swiss National Science Foundation (SNF) [200020_178792] Funding Source: Swiss National Science Foundation (SNF)
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 H-1- and P-31-detected spectroscopic methods. The sensitivity of H-1 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 708 kDa dodecameric DnaB helicase in complex with ADP:AlF4-:DNA, and this despite the very challenging size of the complex.
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