Third piece completes deadly puzzle: Structure of anthrax toxin offers clues to treatment

ema factor appears to provide an ideal drug target. The active site, which mimics adenylyl cyclase, is a deep, narrow pocket that should be comparatively easy to block with a small molecule. It is also very different from mammalian adenylyl cyclase, so there is little risk that the drug would interfere with the normal activity of this important enzyme.

At least two other disease-causing bacteria rely on a similar process: Bordetella pertussis, which causes whooping cough; and Pseudomonas aeruginosa, which infects patients with cystic fibrosis and those with impaired immunity.

Besides it's value in developing better anti-anthrax drugs, the finding is an important one for basic cellular biology. Calcium is not only used for bone formation but also plays a vital role in the communication between cells. Calmodulin is a ubiquitous calcium sensor that interacts with more than 50 protein targets.

"People have studied calmodulin when it is bound to a small piece of various protein targets before," said co-author Andrew Bohm, Ph.D., a crystallography expert at the Boston Biomedical Research Institute, "but the structure of calmodulin with edema factor, a complete protein target, is significantly different from these earlier findings. A lot of the previous studies will have to be reconsidered."

This discovery "is an example of the unexpected benefits of basic science," said Paula Flicker, Ph.D., a program director at the National Institute of General Medical Sciences, which partially supported the work. (The American Heart Association also contributed.)

"Three years ago," said Tang, "when we started this project, Bacillus anthracis was an obscure agricultural pathogen with interesting biological properties. Now anthrax is front and center in every clinician's mind, and within months of the first bioterrorism case we have the s

Contact: John Easton
University of Chicago Medical Center

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