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![[Figure 2]](cb5149fig2mag.jpg)
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Figure 2
Crystal structure of the N-terminal ACDC domain of PfAP2-I. (a) The dimer observed in the asymmetric unit is shown with one subunit represented as a cartoon and the second as a ribbon, both colored in a spectrum. Swapping of helix α4 (red) between the two subunits of is highlighted by red arrows. The ACDC domain of PfAP2-O5, shown as a cartoon colored gray, superimposes on this swapped dimer with a r.m.s.d. of 1.065 Å over 56 aligned Cα atoms. The position of the ACDC and AP2 domains of PfAP2-I is schematized below the structure with their residue ranges. (b) Details of the PfAP2-I swapped dimer interface. Residues involved in stabilizing salt bridges and hydrogen bonds between the facing helices α4 and α2 of the two chains are shown as sticks colored by atom type and labeled. |
![[Figure 2]](cb5149fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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