2K36
Structure ensemble Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments, 1H-15N RDCs and 1H-1H nOe restraints for protein K7 from the Vaccinia virus
Summary for 2K36
| Entry DOI | 10.2210/pdb2k36/pdb |
| NMR Information | BMRB: 15740 |
| Descriptor | Protein K7 (1 entity in total) |
| Functional Keywords | protein, viral protein |
| Biological source | Vaccinia virus (VACV) |
| Total number of polymer chains | 1 |
| Total formula weight | 17488.90 |
| Authors | Kalverda, A.P.,Thompson, G.S.,Vogel, A.,Schr der, M.,Bowie, A.G.,Khan, A.R.,Homans, S.W. (deposition date: 2008-04-22, release date: 2008-10-28, Last modification date: 2024-05-01) |
| Primary citation | Kalverda, A.P.,Thompson, G.S.,Vogel, A.,Schroder, M.,Bowie, A.G.,Khan, A.R.,Homans, S.W. Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3. J.Mol.Biol., 385:843-853, 2009 Cited by PubMed Abstract: Poxviruses have evolved numerous strategies to evade host innate immunity. Vaccinia virus K7 is a 149-residue protein with previously unknown structure that is highly conserved in the orthopoxvirus family. K7 bears sequence and functional similarities to A52, which interacts with interleukin receptor-associated kinase 2 and tumor necrosis factor receptor-associated factor 6 to suppress nuclear factor kappaB activation and to stimulate the secretion of the anti-inflammatory cytokine interleukin-10. In contrast to A52, K7 forms a complex with DEAD box RNA helicase DDX3, thereby suppressing DDX3-mediated ifnb promoter induction. We determined the NMR solution structure of K7 to provide insight into the structural basis for poxvirus antagonism of innate immune signaling. The structure reveals an alpha-helical fold belonging to the Bcl-2 family despite an unrelated primary sequence. NMR chemical-shift mapping studies have localized the binding surface for DDX3 on a negatively charged face of K7. Furthermore, thermodynamic studies have mapped the K7-binding region to a 30-residue N-terminal fragment of DDX3, ahead of the core RNA helicase domains. PubMed: 18845156DOI: 10.1016/j.jmb.2008.09.048 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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