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Fig. 5 | BMC Evolutionary Biology

Fig. 5

From: Insights into the evolution of enzyme substrate promiscuity after the discovery of (βα)8 isomerase evolutionary intermediates from a diverse metagenome

Fig. 5

Structural analysis of CAM1 and CAM2. a. Structural homology model of CAM1, corresponding to a full (βα)8-barrel, and CAM2. The (βα)2 subunit missing in CAM2 is shown in gray. N and C-terminal tails are shown in magenta, loops, alpha helix and beta sheet are marked in green, red and yellow, respectively. b. Structural superposition of CAM2 (gray backbone), CAM2_204, CAM2_R1 and CAM2_R2, where N and C-terminal tails are shown in blue, red, green and orange, respectively. c. Sequence alignment of the 12-amino acid C-terminal variable region of CAM2, CAM2_204 (equivalent to CAM1), CAM2_R1 and CAM2_R2. The pairwise RMSD between CAM1 and CAM2, CAM2 and CAM2_R1, CAM2 and CAM2_R2, and CAM2 and CAM2_204 was 1.73 Å, 1.91 Å, 1.41 Å, 1.73 Å, respectively

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BMC Ecology and Evolution

ISSN: 2730-7182

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