2MU4
Structure of F. tularensis Virulence Determinant
Summary for 2MU4
| Entry DOI | 10.2210/pdb2mu4/pdb |
| NMR Information | BMRB: 25168 |
| Descriptor | flpp3Sol_2 (1 entity in total) |
| Functional Keywords | lipoprotein, membrane protein |
| Biological source | Francisella tularensis subsp. tularensis SCHU S4 |
| Total number of polymer chains | 1 |
| Total formula weight | 13275.47 |
| Authors | Zook, J.J.D.Z.,Mo, G.G.M.,Craciunescu, F.F.C.,Sisco, N.N.S.,Hansen, D.D.H.,Baravati, B.B.B.,Van Horn, W.W.V.H.,Cherry, B.B.C.,Fromme, P.P.F. (deposition date: 2014-09-03, release date: 2015-06-10, Last modification date: 2024-05-15) |
| Primary citation | Zook, J.,Mo, G.,Sisco, N.J.,Craciunescu, F.M.,Hansen, D.T.,Baravati, B.,Cherry, B.R.,Sykes, K.,Wachter, R.,Van Horn, W.D.,Fromme, P. NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins. Structure, 23:1116-1122, 2015 Cited by PubMed Abstract: Tularemia is a potentially fatal bacterial infection caused by Francisella tularensis, and is endemic to North America and many parts of northern Europe and Asia. The outer membrane lipoprotein, Flpp3, has been identified as a virulence determinant as well as a potential subunit template for vaccine development. Here we present the first structure for the soluble domain of Flpp3 from the highly infectious Type A SCHU S4 strain, derived through high-resolution solution nuclear magnetic resonance (NMR) spectroscopy; the first structure of a lipoprotein from the genus Francisella. The Flpp3 structure demonstrates a globular protein with an electrostatically polarized surface containing an internal cavity-a putative binding site based on the structurally homologous Bet v1 protein family of allergens. NMR-based relaxation studies suggest loop regions that potentially modulate access to the internal cavity. The Flpp3 structure may add to the understanding of F. tularensis virulence and contribute to the development of effective vaccines. PubMed: 26004443DOI: 10.1016/j.str.2015.03.025 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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