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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: N-terminal domain replacement changes an archaeal monoacylglycerol lipase into a triacylglycerol lipase

Fig. 1

The three-dimensional structural models (ac) and SDS-PAGE of Ni–NTA affinity-purified TON-LPL and rc-TGL (d). The common structural elements between TON-LPL (a) and rc-TGL (b) are shown in green, the lid domains used in the N-terminal replacement are shown in blue and the 6×-His tag is in red. The catalytic triad amino acid residues for both models are shown as ball and stick with their amino acid positions (a, b). The structural superposition of TON-LPL (green) and rc-TGL (blue) is shown in c. Here a loop of the lid domain in rc-TGL has been shown in red (dotted black circle). SDS-PAGE of the Ni–NTA affinity-purified TON-LPL and rc-TGL is shown in d. Lane 1 is a broad range molecular weight marker and lane 2 is the purified protein and the corresponding purified proteins are named below the SDS-PAGE

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