Convergent evolution in the mechanisms of ACBD3 recruitment to picornavirus replication sites
Fig 2
Detailed view of the interface of the GOLD: EVD68 3A complex.
a-d, Detailed view of the interface between the GOLD domain and the enterovirus-D68 3A protein residues T16-S31 (a), S31-G42 (b), G42-E51 (c), and E51-I58 (d). In the overall view, the protein backbones are shown in cartoon representation; the ACBD3 GOLD domain is depicted in gold, the EVD68 3A protein in light blue. In the detailed view, the amino acid residues from the indicated segments are highlighted in stick representation and colored according to elements—oxygen atoms are colored in red, nitrogens in blue, sulfurs in green, carbons according to the protein assignment. Hydrogen bonds are shown as dotted black lines; hydrogen atoms are not visualized. In the lower left of each panel, hydrogen bonds, non-polar interactions, and salt bridges between the GOLD domain and the EVD68 3A protein are listed. The distance cut-off used for hydrogen bonds is 3.3 Å, and for non-polar interactions and salt bridges 4.0 Å. In the case of non-polar interactions, only the closest atom pair for each pair of residues is listed.