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Figure 1


Fig. 1. (A) Amino acid (aa) sequence alignment of conserved elements among different endonuclease active sites. Conserved aa residues are highlighted in red. Most known endonucleases have the conserved R(K)GH triad. CuquEndo also contains other aa residues implicated in the nucleophilic attack of DNA substrate and stabilization of the active site. (B) Molecular modeling of CuquEndo and active site comparison with Smarcens endonuclease (PDB id 1G8T). The similarity of the active site geometry suggests that both enzymes might have a similar mechanism of action on DNA substrates. (C) Phylogenetic analysis of the endonuclease family. The unrooted neighbor-joining tree (10,000 bootstraps) was generated by MEGA 3.1 software. CuquEndo, Culex quinquefasciatus; Smarcens, Serratia marcescens; Mjaponic, Marsupenaeus japonicus; Pcamtsch, Paralithodes camtschaticus; Hsapiens, Homo sapiens; Gmorsitans, Glossina morsitans; Longipalpis, Lutzomyia longipalpis; Pariasi, Phlebotomus ariasi; Agambiae, Anopheles gambiae. NCBI accession numbers in parentheses.





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