Fig. 5: Conformational differences in the ADP-bound and ADP-BeFx-bound states.
From: Structural insights into histone exchange by human SRCAP complex
a Superimposition of the two structures with differences highlighted and indicated with arrows. Nucleosomes are superimposed for comparison. Three views showing the rotation/displacement of SRCAP, hexamer, and ARP6–ZNHIT1 dimer, respectively. b–d Close-up views of the differences in ZNHIT1 (b) H2A C-terminal tail (c) and YL1 (d). Conformational differences are highlighted with arrows. Structural comprision showing the dissociation of ZNHIT1 from the motor-proximal H2A–H2B (b). Structural comparison showing the displacement of ARP6 and the possible interaction between the relocated ARP6 and the C-terminal tail of histone H2A and the sequence alignment of the C-terminal tail of H2A and H2A.Z. The subdomain4 of ARP6 is shown in electrostatic surface and H2A tails (residues 110–127) are shown in transparent surfaces and structural models (c). Structural comparison showing the contraction of YL1 (d).
