Autor: |
Alexander A. Malär, Nino Wili, Laura A. Völker, Maria I. Kozlova, Riccardo Cadalbert, Alexander Däpp, Marco E. Weber, Johannes Zehnder, Gunnar Jeschke, Hellmut Eckert, Anja Böckmann, Daniel Klose, Armen Y. Mulkidjanian, Beat H. Meier, Thomas Wiegand |
Jazyk: |
angličtina |
Rok vydání: |
2021 |
Předmět: |
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Zdroj: |
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021) |
Druh dokumentu: |
article |
ISSN: |
2041-1723 |
DOI: |
10.1038/s41467-021-25599-z |
Popis: |
Here, the authors use solid-state NMR and EPR measurements to characterise the ATP hydrolysis transition state of the oligomeric bacterial DnaB helicase from Helicobacter pylori, which was trapped by using aluminium fluoride as a chemical mimic. They identify protein protons that coordinate to the phosphate groups of ADP and DNA and observe that the aluminium fluoride unit is highly mobile and fast-rotating. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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