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. 2021 Dec 1;12:7001. doi: 10.1038/s41467-021-27295-4

Fig. 2. Structural models elucidate the conformational switching of Rad26 in response to nucleotide binding and its crucial role in transcription bubble remodeling.

Fig. 2

a View of the Rad26 active site with bound ATP. b View of the Rad26 active site with bound ADP. The binding pocket is shown in gray. Nucleotides are shown in ball-and-stick representation (cyan). Select residues making key contacts with the nucleotide are shown in stick representation (green). Red dash lines denote hydrogen bonds. Mg (dark brown sphere) is coordinated by D469, D470 and ATP/ADP phosphate (red dash lines). (c, e, g) Residue contacts at the RecA1 and RecA2 interface in (c), apo state; (e), ATP state; (g), ADP state. (d, f, h) Residue contacts mapped onto the RecA1 and RecA2 surface in (d). apo state; (f), ATP state; (h), ADP state. The side chains of contact forming residues are shown with salt–bridge interactions in red and blue, hydrogen bonding interactions between polar residues in cyan and light blue, and hydrophobic interactions in orange and purple.