journal menu
![[Figure 5]](cb5156fig5mag.jpg)
|
|
Figure 5
Structure of ALC1 in an open conformation, bound to a PARylated nucleosome. (a) Cryo-EM map colored by chain assignment, following the color codes from Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif){kind=small} (a) for the nucleosome and Fig. 2(a) for ALC1. (b) Atomic model, shown in the same orientations and with the same color code as the map shown in (a). (c) Structure of the auto-inhibited state. The antibody used for crystallization is shown as a translucent cyan surface. From PDB entry 7epu. (d) Structure of the intermediate state (dyad view). From this study. (e) Structure of the active state. From PDB entry 8b0a. In (c), (d) and (e), the ATPase residues mutated in the study by Lehmann et al. (2017) are shown as spheres. In (c) and (d), the macro domain residues Arg857 and Arg860, found mutated in cancer, are shown as spheres and labeled, and the ADPr-binding pocket of the macro domain is indicated by an ADPr molecule (shown in ball-and-stick representation) modeled by structural superimposition of the structure of the Af1521–ADPr complex from PDB entry 2bfq (the Af1521 protein is not shown for clarity). In (b), (d) and (e), the nucleosome is shown as a translucent surface for clarity. See also Supplementary Fig. S2 for the validation of this cryo-EM map (including local resolution and orientation distribution). See also Supplementary Fig. S3 for a movie of an interpolation between the closed and open conformations of nucleosome-bound ALC1. |
![[Figure 5]](cb5156fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
