Crystal Structure of Vaccinia Viral A27 Protein Reveals a Novel Structure Critical for Its Function and Complex Formation with A26 Protein
Figure 2
Interactions of the N-terminal region (NTR) and the C-terminal region (CTR) interfaces.
(A) The residues in the CTR interface are depicted as sphere models (chain A′, light blue; ′ chain B′, light cyan). They are divided into two layers of cross-sections (C-S) for hydrophobic interaction and one hydrogen-bonding interaction. The hydrophobic resides involved in the NTR interface are shown as a cluster of spheres in blue (chain A), cyan (chain B), and magenta (chain C), and divided into 8 layers of C-S. The filled circles denote the C-terminus and the open circles indicate the N-terminus of tA27. The triple L-to-A mutation sites at the NTR interface are boxed. (B) The 2| FO|-|FC| electron density maps are contoured at 1.0σ level as green mesh, and the refined protein model is shown as sticks in blue (chain A′), cyan (chain B′), magenta (chain C), light blue (chain A′), and light cyan (chain B′).