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. 2014 Nov 3;111(46):16359–16364. doi: 10.1073/pnas.1410806111

Fig. 1.

Fig. 1.

Sequence and structural features of TteCas3. (A) Summarized organization of 944-aa TteCas3 HD nuclease, SF2 helicase, and CTD, highlighting features described in Results. Shown are five residues of the HD domain that coordinate metal ions and water for nuclease activity (Fig. 2B). Residues that were mutagenized to abolish nuclease and ATPase activities (Fig. 2 C and E) are underlined. Other features of Cas3 structure function, detailed in Results, are labeled WF motif, β-hairpin and motifs Ic, IV, and VI. (B) Sequence alignment of conserved regions. Residues that interact with catalytic metal ions and a water molecule are indicated by asterisks, and conserved helices motifs are marked (I–VI). E.co, E. coli K-12; M.ja, M. jannaschii DSM 2661; P.ae, Pseudomonas aeruginosa; S.mu, S. mutans NN2025; S.th, S. thermophilus; T.te, T. terrenum; T.th, T. thermophilus HB8.