Extended Data Fig. 8: Sequence alignment of BRCT domains from various proteins. | Nature Structural & Molecular Biology

Extended Data Fig. 8: Sequence alignment of BRCT domains from various proteins.

From: Cryo-EM structure of the Rev1–Polζ holocomplex reveals the mechanism of their cooperativity in translesion DNA synthesis

Extended Data Fig. 8

Amino acid sequence alignment of conventional as well as DNA binding BRCT domains is shown. Equivalent residues among all the BRCTs are highlighted in yellow. Secondary structure elements of the Rev1 N-helix-BRCT module are shown above and are derived from the coordinates of Rev1-Polζ holocomplex structure (PDB ID: 8TLQ) using ESpript. Helices are designated as black coils and beta sheets are indicated by blue arrows. Key DNA binding residues in Rev1 BRCT are highlighted by a purple star and those conserved between the yeast and human Rev1 BRCT are highlighted in red.

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