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New protein fold revealed by a 1.65 Å resolution crystal structure of Francisella tularensis pathogenicity island protein IglC
Author(s) -
Sun Ping,
Austin Brian P.,
Schubot Florian D.,
Waugh David S.
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.073177307
Subject(s) - francisella tularensis , tularemia , pathogenicity island , francisella , microbiology and biotechnology , biology , phagosome , biogenesis , intracellular , bacteria , virulence , genetics , salmonella , gene
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 β‐sandwich conformation that exhibits no similarity with any known protein structure.