Fig. 4: Comparison of Abo1 cryo-EM structures in the ATP and ADP states reveal a hexameric spiral-to-ring transition.
From: Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone
a Cryo-EM maps of Abo1 in the ATP, ADP, and apo states showing the “top” (AAA1), “side”, and “bottom” (AAA2) face of the AAA+ hexamer. Resolution of ATP, ADP, and apo structures are at 3.5 Å, 4.4 Å, and 6.9 Å respectively. Electron density above the AAA+ ring is assigned as the bromodomain. The top view is clipped underneath the bromodomain to show the upper surface of the AAA1 domains. A top view of the apo-Abo1 bromodomain is shown in Supplementary Fig. 12. b Structures of Abo1 in the ATP state, and flexible-fitted Abo1 models in the ADP and apo state. The Abo1 hexamer is colored according to subunit (chains A–F).
