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. 2018 Oct 26;46(22):12008–12021. doi: 10.1093/nar/gky1011

Figure 4.

Figure 4.

Structure of the MARF1 NYN domain. (A) Comparative sequence analysis of the NYN domains of human (Hs), Xenopus tropicalis (Xt), Danio rerio (Dr), Lasius niger (Ha) and Apis mellifera (Am) MARF1 orthologs. The multiple sequence alignment was generated using MAFFT version 7 and formatted using Jalview (49,50). Secondary structure elements with corresponding numbering are indicated above the sequence. Invariant residues are coloured dark blue while conservative substitutions are depicted in shades of light blue. (B) Left, Crystal structure of the MARF1 NYN domain shown in cartoon and surface representations. Right, cartoon representation of the MARF1 NYN domain, with invariant active site residues depicted in stick format. (C) Structural superpositions of the human MARF1 NYN domain with the NYN domain of Bacillus subtilis YacP/Rae1 (PDB 5MQ8), and the PIN domains of human SMG6 (PDB 2HWW) and MCPIP1 (PDB 3V34). The structures were superimposed using the DALI server (51) and are shown in identical orientations. (D) Zoom-in view of the NYN domain ribonuclease active site of MARF1, overlaid with the structures of human SMG6 and MCPIP1 PIN domains. Invariant active site residues are shown in stick format. The bound magnesium ion present in the MCPIP1 structure is depicted as a purple sphere.