Extended Data Fig. 9: Conformational changes in the head segment between the apo and +ATP states.
From: Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism
a, Structural alignment based on the RecA-like lobe of the Smc2 head domains of the +ATP (‘open coils’) form (in blue colors) and the apo (nucleotide-free) form (grey colors) highlights the extent of coiled-coil kinking in Smc2. Positioning and extent of the kinking in the carboxy-terminal Smc2 coiled coil are indicated. b, Simultaneous Smc2–Smc4 head engagement and Ycs4 binding to Smc4 would lead to steric clashes. c, Simultaneous binding of Ycs4 and Ycg1 HEAT-repeat subunits to the Smc4 and Smc2 heads, respectively, in the non-engaged state would result in major steric clashes.
