Journal
PROTEIN SCIENCE
Volume 16, Issue 11, Pages 2560-2563Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1110/ps.073177307
Keywords
Francisella tularensis; IglC; crystal structure; bioterrorism
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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 angstrom resolution. IglC adopts a beta-sandwich conformation that exhibits no similarity with any known protein structure.
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