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Biology of infection: A bacterial ballistic system
Date:6/20/2014

icularly interested in elucidating the mechanism of contraction of the complex, which does not require input of metabolic energy." To answer both of these questions, it is essential to obtain a more detailed picture of the structure of the complex and Wendler and her associates have taken a significant step in that direction.

"We were able to determine the structure of the contracted form of the outer sheath complex at sub-nanometer resolution. It turns out that its basic architecture and the structural elements that stabilize the complex are related to those of certain proteins found in bacterial viruses, but have been modified in the course of evolution to enable them to serve a secretory function," as Wendler explains. Notably, in the contracted form of the complex studied by Wendler and her colleagues, the recognition site for ClpV, a protein that recycles the subunits of the tubular complex after ejection of effector proteins, is exposed and available for binding. In contrast, in a model of the extended configuration, this site is inaccessible. This neatly explains why the sheath is disassembled only after the toxins have been injected into the target cell.

Wendler and her team now plan to improve the resolution of the structural data still further, and to characterize in detail the conformation of the contractile apparatus in its extended state, so to gain insight into the mechanism responsible for the contraction process itself. "A comprehensive understanding of the structure and function of all the components of this molecular machine could facilitate the development of new, effective antibiotics," Wendler concludes.


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Contact: Luise Dirscherl
presse@lmu.de
0049-892-180-3423
Ludwig-Maximilians-Universitt Mnchen
Source:Eurekalert

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