Extended Data Figure 3: Structural comparisons among Snf2, Chd1, and ISWI. | Nature

Extended Data Figure 3: Structural comparisons among Snf2, Chd1, and ISWI.

From: Structure and regulation of the chromatin remodeller ISWI

Extended Data Figure 3

a, b, Comparisons of the overall structures of MtISWI and MtSnf2 (Protein Data Bank accession number 5HZR)13. The structures of the core2 domains are aligned. The core1 domains are shown as surface presentations, which orient differently in these two proteins. ISWI is coloured as in Fig. 1. The core1 and SnAc domains of MtSnf2 are coloured grey and blue, respectively. Motif V (R567 of MtISWI and R950 of MtSnf2) and the acidic patch of the core2 domain implicated in H4-binding are coloured gold. c, d, Comparisons of the overall structures of MtISWI and ScChd1 (Protein Data Bank accession number 3MWY)12. The structures of the core2 domains are aligned. The core1 domains are shown as surface presentations. The N-terminal dCD and the C-terminal bridge of ScChd1 are coloured pink and red, respectively. The NegC domain of ISWI extends outwards, whereas the C-terminal bridge of Chd1 binds to the core1 domain intramolecularly. e, Structural alignment of the core1 domains of MtISWI (green), MtSnf2 (blue), and ScChd1 (grey). f, Structural alignment of the core2 domains of MtISWI (cyan), MtSnf2 (blue), and ScChd1 (grey). The DNA-binding elements identified in MtSnf2 (K662 and R950) and ScChd1 (R750 and R772) are conserved among these remodellers, whereas K692 of MtSnf2 is unique to the Snf2-subfamily proteins. The arginine-fingers of MtISWI (R599 and R602), MtSnf2 (R982 and R985), and ScChd1 (R804 and R807) are conserved (Extended Data Fig. 1). The Brace helices of the remodellers show different lengths. g, Comparisons of lobe1 of MtISWI, MtSnf2 and ScChd1. The structures of the core1 domains are aligned. The N-terminal auxiliary domains of MtISWI (AutoN), MtSnf2 (postHSA), and ScChd1 (dCD) interact with the core1 domain differently. h, Comparisons of lobe2 of MtISWI, MtSnf2, and ScChd1. The structures of the core2 domains are aligned. The C-terminal auxiliary domains of MtISWI (NegC), MtSnf2 (SnAC), and ScChd1 (bridge) interact with the core2 domain differently.

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