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. 2000 Jun 15;19(12):3110–3118. doi: 10.1093/emboj/19.12.3110

graphic file with name cdd299f1.jpg

Fig. 1. Structure of the NaeI monomer. (A) Ribbon diagram: α-helices in cyan, 310 helices in blue and β-strands in green. The N-terminal (Endo) domain has topology similar to other restriction endonucleases. The C-terminal (Topo) domain contains a CAP or helix–turn–helix motif (H7, H8, 310 helix before H9, B10, B11) for DNA binding. The hinge loop is around Gln170. L43 is shown in ball-and-stick representation. (B) Sequence and secondary structure of NaeI. Cyan cylinders and green arrows represent α-helices and β-strands, respectively. The helices H4a and H4b are bent at Met65.