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5evg

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<StructureSection load='5evg' size='340' side='right' caption='[[5evg]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='5evg' size='340' side='right' caption='[[5evg]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5evg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EVG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5evg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"francisella_tularensis_subsp._novicida"_(larson_et_al._1955)_sjostedt_2005 "francisella tularensis subsp. novicida" (larson et al. 1955) sjostedt 2005]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EVG FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5evf|5evf]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5evf|5evf]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACX55_1794 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264 "Francisella tularensis subsp. novicida" (Larson et al. 1955) Sjostedt 2005])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5evg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5evg OCA], [http://pdbe.org/5evg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5evg RCSB], [http://www.ebi.ac.uk/pdbsum/5evg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5evg ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5evg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5evg OCA], [http://pdbe.org/5evg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5evg RCSB], [http://www.ebi.ac.uk/pdbsum/5evg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5evg ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Francisella tularensis is a highly virulent Gram-negative intracellular pathogen capable of infecting a vast diversity of hosts, ranging from amoebae to humans. A hallmark of F. tularensis virulence is its ability to quickly grow to high densities within a diverse set of host cells, including, but not limited to, macrophages and epithelial cells. We developed a luminescence reporter system to facilitate a large-scale transposon mutagenesis screen to identify genes required for growth in macrophage and epithelial cell lines. We screened 7,454 individual mutants, 269 of which exhibited reduced intracellular growth. Transposon insertions in the 269 growth-defective strains mapped to 68 different genes. FTT_0924, a gene of unknown function but highly conserved among Francisella species, was identified in this screen to be defective for intracellular growth within both macrophage and epithelial cell lines. FTT_0924 was required for full Schu S4 virulence in a murine pulmonary infection model. The DeltaFTT_0924 mutant bacterial membrane is permeable when replicating in hypotonic solution and within macrophages, resulting in strongly reduced viability. The permeability and reduced viability were rescued when the mutant was grown in a hypertonic solution, indicating that FTT_0924 is required for resisting osmotic stress. The DeltaFTT_0924 mutant was also significantly more sensitive to beta-lactam antibiotics than Schu S4. Taken together, the data strongly suggest that FTT_0924 is required for maintaining peptidoglycan integrity and virulence.
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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 A 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.
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Identifying Francisella tularensis genes required for growth in host cells.,Brunton J, Steele S, Miller C, Lovullo E, Taft-Benz S, Kawula T Infect Immun. 2015 Aug;83(8):3015-25. doi: 10.1128/IAI.00004-15. Epub 2015 May, 18. PMID:25987704<ref>PMID:25987704</ref>
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Structure of the conserved Francisella virulence protein FvfA.,Kolappan S, Lo KY, Shen CLJ, Guttman JA, Craig L Acta Crystallogr D Struct Biol. 2017 Oct 1;73(Pt 10):814-821. doi:, 10.1107/S205979831701333X. Epub 2017 Sep 27. PMID:28994410<ref>PMID:28994410</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

Revision as of 06:35, 20 December 2017

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

5evg, resolution 1.82Å

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