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. Author manuscript; available in PMC: 2020 Aug 17.
Published in final edited form as: Nat Struct Mol Biol. 2020 Feb 17;27(3):233–239. doi: 10.1038/s41594-020-0379-7

Extended Data Fig. 3. Comparative structural analysis of the cohesin ATPase.

Extended Data Fig. 3

a, Structural alignment-based superposition of the RecA N-lobes of apo CtSmc1–CScc1 (red) and ATPγS-bound ySmc1–CScc1 complex (grey; PDB code 1W1W). Cα root-mean-square deviation [RMSD] = 0.98 Å. b, The Smc3–NScc1 ATPγS complex (PDB code 4UX3). c, Relative motions of α-helices within the ctSmc1 ATPase upon ATPγS binding and head heterodimerization. d, Relative motions of α-helices within the ySmc3 ATPase upon ATPγS binding and head heterodimerization. e, The cross-links are positioned in loops between secondary structural elements. f, Structural details around the cross-linked disulfides. Smc3 N1204 and CtSmc1 L1160 are closely apposed in the modeled heterodimer (grey). Replacement of these residues by cysteine allows cross-linking without major distortions in the Smc heterodimer. The cystine disulfide bonds are indicated in yellow.