5EVG

Crystal structure of a Francisella virulence factor FvfA in the orthorhombic form

Summary for 5EVG

• Entry DOI: 10.2210/pdb5evg/pdb
• Related: 5EVF
• Descriptor: Francisella virulence factor (2 entities in total)
• Functional Keywords: francisella tularensis, virulence factor, unknown function
• Biological source: Francisella novicida
• Total number of polymer chains: 1
• Total formula weight: 11902.31

Authors

Kolappan, S.,Lo, K.Y.,Shen, C.L.J.,Guttman, J.A.,Craig, L. (deposition date: 2015-11-19, release date: 2016-10-26, Last modification date: 2024-10-30)

Primary citation

Kolappan, S.,Lo, K.Y.,Shen, C.L.J.,Guttman, J.A.,Craig, L.
Structure of the conserved Francisella virulence protein FvfA.
Acta Crystallogr D Struct Biol, 73:814-821, 2017

PubMed 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 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.

PubMed: 28994410
DOI: 10.1107/S205979831701333X

Experimental method

X-RAY DIFFRACTION (1.82 Å)