Fig. 3: Structure of Rv2067c and its comparison to DOT1L.
a Crystal structure of Rv2067c. The asymmetric unit contains two molecules of Rv2067c related by two-fold symmetry and the two-fold axis is perpendicular to the page, shown as biconvex sign (maroon). b, c Each monomer is composed of catalytic domain (CD), dimerization domain (DD, composed of large subdomain, LSD and small subdomain, SSD) and C-terminal domain (CTD). Dimer is formed by cross-subdomain interactions between the DDs. SAH is depicted as spheres. a, b The broken lines represent the missing electron density (disordered regions). The substrate-binding troughs are indicated with arrowheads (yellow). d Schematic of domain organization in Rv2067c (top) and DOT1L (bottom). e Crystal structure of DOT1L (PDB: 1NW3). Residues 5–332 are structured (DOT1L3D). The DOT1L3D contains an N-terminal portion and a catalytic core. SAM is depicted as spheres. f Full length human DOT1L (1537 aa) structure model (AlphaFold2 model, AF-Q8TEK3-F1). The structured part of the catalytic domain (DOT1L3D) is rendered as surface and the remaining region as cartoon, which is disordered with interspersed α-helices (CC0–CC3) that form coiled-coil (CC) structures with the interacting partners. The model is colored according to the AlphaFold2 prediction confidence. The low confidence score indicates intrinsic disorder. The N- and C-termini are labeled as N and C, respectively. SAH S-adenosyl-L-homocysteine, SAM S-adenosyl-L-methionine. Scale bars 10 Å.
