Acta Crystallographica Section D: Structural Biology
Acta Crystallographica Section D: Structural Biology
5 years ago

Structure of the conserved Francisella virulence protein FvfA

Structure of the conserved Francisella virulence protein FvfA
Karen Y. Lo, Subramania Kolappan, Lisa Craig, Julian A. Guttman, Chiao Ling Jennifer Shen
Francisella tularensis is a potent human pathogen that invades and survives in macrophage and epithelial cells. Two identical proteins, FTT_0924 from F. tularensis subsp. tularensis and FTL_1286 from F. tularensis subsp. holarctica LVS, have previously been identified as playing a role in protection of the bacteria from osmotic shock and its survival in macrophages. FTT_0924 has been shown to localize to the inner membrane, with its C-terminus exposed to the periplasm. Here, crystal structures of the F. novicida homologue FTN_0802, which we call FvfA, in two crystal forms are reported at 1.8 Å resolution. FvfA differs from FTT_0924 and FTL_1286 by a single amino acid. FvfA has a DUF1471 fold that closely resembles the Escherichia coli outer membrane lipoprotein RscF, a component of a phosphorelay pathway involved in protecting bacteria from outer membrane perturbation. The structural and functional similarities and differences between these proteins and their implications for F. tularensis pathogenesis are discussed.1.8 Å resolution crystal structures of a Francisella protein required for growth in host cells are reported.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1107/S205979831701333X

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