Structure of the conserved Francisella virulence protein FvfA
Back to previous page
| Authors: | Kolappan, S; Lo, KY; Shen, CLJ; Guttman, JA; Craig, L |
| Year: | 2017 |
| Journal: | Acta Crystallogr. Sect. D-Struct. Biol. 73: 814-821 Article Link (DOI) |
| Title: | Structure of the conserved Francisella virulence protein FvfA |
| Abstract: | 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 angstrom 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. |
Departmental members may update their publication list.