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Published online before print September 28, 2007, 10.1110/ps.073177307
Protein Science (2007), 16:2560-2563. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

New protein fold revealed by a 1.65 Å resolution crystal structure of Francisella tularensis pathogenicity island protein IglC

Ping Sun, Brian P. Austin, Florian D. Schubot1, and David S. Waugh

Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland 21702-1201, USA

(RECEIVED August 16, 2007; FINAL REVISION August 16, 2007; ACCEPTED August 22, 2007)

Francisella tularensis is a highly infectious Gram-negative intracellular pathogen that causes the fulminating disease tularemia and is considered to be a potential bioweapon. F. tularensis pathogenicity island proteins play a key role in modulating phagosome biogenesis and subsequent bacterial escape into the cytoplasm of macrophages. The 23 kDa pathogenicity island protein IglC is essential for the survival and proliferation of F. tularensis in macrophages. Seeking to gain some insight into its function, we determined the crystal structure of IglC at 1.65 Å resolution. IglC adopts a beta-sandwich conformation that exhibits no similarity with any known protein structure.

Keywords: Francisella tularensis ; IglC; crystal structure; bioterrorism


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[Abstract] [Full Text] [PDF]


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