PDBsum entry 2k36

Viral protein

PDB id: 2k36

Contents

Protein chain

149 a.a.

PDB id:

2k36

Name:

Viral protein

Title:

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

Structure:

Protein k7. Chain: a. Engineered: yes

Source:

Vaccinia virus. Vacv. Strain: wr western reserve / wr. Gene: k7r. Expressed in: escherichia coli. Other_details: the pet15 vector was modified to replace the thrombin cleavage site with an rtev cleavage site

NMR struc:

15 models

Authors:

A.P.Kalverda,G.S.Thompson,A.Vogel,M.Schr Der,A.G.Bowie,A.R.Khan, S.W.Homans

Key ref:

A.P.Kalverda et al. (2009). 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. PubMed id: 18845156 DOI: 10.1016/j.jmb.2008.09.048

Date:

22-Apr-08 Release date: 28-Oct-08

Protein chain

P68466  (K7_VACCW) -  Protein K7 from Vaccinia virus (strain Western Reserve)

Seq: 149 a.a.

Struc: 149 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2008.09.048

J Mol Biol 385:843-853 (2009)

PubMed id: 18845156

Poxvirus K7 Protein Adopts a Bcl-2 Fold: Biochemical Mapping of Its Interactions with Human DEAD Box RNA Helicase DDX3.

A.P.Kalverda, G.S.Thompson, A.Vogel, M.Schröder, A.G.Bowie, A.R.Khan, S.W.Homans.

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.

Selected figure(s)

Figure 3.
Fig. 3. The BH3 groove of K7 is filled with hydrophobic side chains. The orientation is the same as in Fig. 1. K7 is coloured green, and N1 is grey. Side chains are represented as stick models to emphasize BH3 groove closure by Y67, Y68, and F89 in K7. The N1 surface is relatively open, although Arg58 of α4 resides along one wall of the BH3 groove.

Figure 9.
Fig. 9. Viral proteins that adopt the Bcl-2 fold. The family can be subdivided into two structural groups, those that have a closed BH3 groove (K7, and likely A52, whose structure is currently unknown) and N1/M11/M11L, which have open grooves.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2009, 385, 843-853) copyright 2009.

Figures were selected by an automated process.