In mapping the structure of short-lived bacterial 'switches,' biochemist may find novel answer to antibiotic resistance

a common two-component system wherein a biological signal prompts a histidine molecule on one component to transfer a phosphate ion to an aspartate molecule on a second component. A strikingly similar two-component mechanism operates among many species of bacteria. "Our goal was to unravel the structural basis of the switch in the signal cascade at atomic resolution, with the hopes of developing new approaches for treating multiple-resistant infections," Kern says.

It's the first time the structure of such a short-lived protein has ever been pinpointed by scientists, Kern says, and heralds new possibilities for future NMR imaging of other evanescent biomolecules.

Key to the research was an innovative approach to nuclear magnetic resonance (NMR) spectroscopy that allowed Kern to regenerate, for a day and a half, the fleeting active configuration the protein switch normally assumes only during the few minutes when it grabs and holds a phosphate ion. The rapid loss of these ions -- necessary for fast responses to the environment -- usually makes the active, phosphate-bound form of the switch far too transient for structural analysis. To keep the protein switch in its active state long enough to get a good snapshot, Kern collected NMR spectra on the protein during catalysis using a constant stream of phosphate.

Kern's co-authors on the paper are Brian F. Volkman of the University of Wisconsin, Sydney Kustu of the University of California at Berkeley, and Peter Luginbhl, Michael J. Nohaile, and David E. Wemmer of the Lawrence Berkeley National Laboratory. The research was sponsored by the U.S. Department of Energy and the National Science Foundation.


Contact: Steve Bradt
Brandeis University

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