New kinase regulation mechanism found in HipBA: a bacterial persistence switch
✍ Scribed by Evdokimov, Artem ;Voznesensky, Igor ;Fennell, Kimberly ;Anderson, Marie ;Smith, James F. ;Fisher, Douglas A.
- Publisher
- International Union of Crystallography
- Year
- 2009
- Tongue
- English
- Weight
- 453 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0907-4449
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✦ Synopsis
Bacterial persistence is the ability of individual cells to randomly enter a period of dormancy during which the cells are protected against antibiotics. In Escherichia coli, persistence is regulated by the activity of a protein kinase HipA and its DNA-binding partner HipB, which is a strong inhibitor of both HipA activity and hip operon transcription. The crystal structure of the HipBA complex was solved by application of the SAD technique to a mercury derivative. In this article, the fortuitous and interesting effect of mercury soaks on the native HipBA crystals is discussed as well as the intriguing tryptophan-binding pocket found on the HipA surface. A HipA-regulation model is also proposed that is consistent with the available structural and biochemical data.