2021
DOI: 10.1038/s41467-021-25599-z
| View full text |Cite
|
Sign up to set email alerts
|

Abstract: The ATP hydrolysis transition state of motor proteins is a weakly populated protein state that can be stabilized and investigated by replacing ATP with chemical mimics. We present atomic-level structural and dynamic insights on a state created by ADP aluminum fluoride binding to the bacterial DnaB helicase from Helicobacter pylori. We determined the positioning of the metal ion cofactor within the active site using electron paramagnetic resonance, and identified the protein protons coordinating to the phosphat… Show more

Help me understand this report
View preprint versions

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
18
0

Year Published

2022
2022
2023
2023

Publication Types

Select...
5
1

Relationship

2
4

Authors

Journals

citations
Cited by 12 publications
(18 citation statements)
references
References 108 publications
0
18
0
Order By: Relevance
“…We have recently presented the first hPH correlation spectrum recorded at 100 kHz MAS in the context of a large motor protein coordinating to DNA and ADP to probe hydrogen bonding. 11 To establish and setup such experiments, we have chosen a small model compound as an external standard, namely the phosphorylated amino acid tyrosine ( ortho -phospho-tyrosine) which has already been subject to solid-state NMR studies. 96,97 Figure S8 summarizes the 1 H MAS spectra, the proton line broadening contributions measured at 100 kHz MAS as well as the hPH spectra (for more details see the Section S2, ESI†).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…We have recently presented the first hPH correlation spectrum recorded at 100 kHz MAS in the context of a large motor protein coordinating to DNA and ADP to probe hydrogen bonding. 11 To establish and setup such experiments, we have chosen a small model compound as an external standard, namely the phosphorylated amino acid tyrosine ( ortho -phospho-tyrosine) which has already been subject to solid-state NMR studies. 96,97 Figure S8 summarizes the 1 H MAS spectra, the proton line broadening contributions measured at 100 kHz MAS as well as the hPH spectra (for more details see the Section S2, ESI†).…”
Section: Resultsmentioning
confidence: 99%
“…6,7 We herein introduce phosphorus-31 as an additional radiofrequency channel in proton-detected fast MAS experiments (≥100 kHz) 6–8 allowing the investigation of a variety of functionalized phosphorus-containing materials (for instance, heterogeneous catalysts, modified zeolites 9 or aluminophosphates 10 ), as well as the characterization of biomolecular protein–nucleotide complexes. 11 Compared to previously reported 31 P-detected 1 H– 31 P heteronuclear correlation experiments (HETCOR) combined with rather high-power 1 H homonuclear decoupling performed at relatively slow MAS frequencies, 9,12–15 the herein proposed 1 H-detected 31 P– 1 H correlation experiment at fast MAS benefits in particular from requiring small sample amounts (<0.5 mg) and low-power decoupling. In addition, inverse detection schemes as used in solution (where one starts and ends with proton polarization) is turning into the method-of-choice at fast MAS frequencies due to the high sensitivity in 1 H-detection of the NMR probes for small rotor diameters.…”
Section: Introductionmentioning
confidence: 85%
“…The approaches used so far to characterize intermolecular contacts in nucleic acid–protein complexes can be divided in three classes, whereby many of the published studies use a combination of these approaches. Similar to solution-state NMR, the involvement of a molecular surface in interactions with a binding partner can be detected by either chemical shift perturbations (CSPs) or intensity changes of the ssNMR peaks of the surface atoms, when comparing the free and the bound-state of the molecule ( Ahmed et al, 2020 , Boudet et al, 2019 , Lacabanne et al, 2020 , Malär et al, 2021b , Wiegand et al, 2020b , Wiegand et al, 2019 , Wiegand et al, 2016 , Williamson, 2013 ). For example, the formation of an hydrogen bond at a nucleic acid–protein interface causes a downfield shift of the involved 1 H atom ( Wagner et al, 1983 ).…”
Section: Characterization Of Nucleic Acid–protein Interfaces By Mas S...mentioning
confidence: 99%
“…The chemical shifts of residues in (D) have a larger dependence on temperature and are thus not involved in hydrogen bonds. Figures (C–D) are reproduced from ( Malär et al, 2021b ) ©2021 with permission from Springer Nature. …”
Section: Chemical Shift Perturbations and Intensity Changesmentioning
confidence: 99%
See 1 more Smart Citation