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. Author manuscript; available in PMC: 2014 Aug 17.
Published in final edited form as: Methods Mol Biol. 2014;1123:191–221. doi: 10.1007/978-1-62703-968-0_14

Fig. 8.

Fig. 8

Structural representation of areas for optimization of partially active chimeras. (a) The I-OnuI structure (gray) is shown with superimposed LAGLIDADG helices from five different enzymes: I-OnuI helices are colored purple, I-LtrI are green, I-MpeMI (homology model) are cyan, I-PanMI are magenta, and I-GzeII are yellow. Side chains are depicted as “sticks” at the DNA-distal end of the LAGLIDADG helices. A magnified view highlights the lack of conservation at these positions. (b) A significant portion of the chimeric interface is formed between the two adjacent LAGLIDADG helices. Residues from a single parent enzyme (blue) can be substituted onto BOTH sides of the LAGLIDADG interface to help overcome problems with an otherwise incompatible chimeric interface