Fig. 4: Structural comparison between AsfvAP and homologous proteins.
From: A unique DNA-binding mode of African swine fever virus AP endonuclease
a Superposition of AsfvAP, BaNfo, MtEndoIV, and TtNfo structures. b, c Superposition of AsfvAP/DNA-1 and EcNfo/substrate (PDB: 2NQJ) complexes. d Superposition of the DNAs bound in the active sites of AsfvAP/DNA-1, EcNfo/product (PDB: 2NQ9), and EcNfo/substrate complexes. In panels a, b, AsfvAP, BaNfo, MtEndoIV, TtNfo, and EcNfo are colored in white, cyan, yellow, orange, and pink, respectively. The R1–R3 regions are colored in green for AsfvAP, whereas they are colored in blue for all other proteins. In panel c, AsfvAP and EcNfo are colored in white and pink, respectively. For the AsfvAP/DNA-1 complex, the uncleaved strand, upstream and downstream of the cleaved strand are colored in red, blue and yellow, respectively. Zn2+ ions are shown as black spheres. For the EcNfo/substrate complex, DNA strands and Zn2+ ions are all colored in cyan. In panel d, DNA, protein, and Zn2+ ions are colored in atomic colors (C, white; N, blue; O, red; P, orange; Zn2+, black) for the AsfvAP/DNA-1 complex. The EcNfo/product complex is colored in green. For the EcNfo/substrate complex, DNA is colored in cyan, protein and Zn2+ ions are colored in pink.
