Publication Abstract from PubMed
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.
New kinase regulation mechanism found in HipBA: a bacterial persistence switch.,Evdokimov A, Voznesensky I, Fennell K, Anderson M, Smith JF, Fisher DA Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):875-9. Epub 2009, Jul 17. PMID:19622872[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
