Fig. 3 | Scientific Reports

Fig. 3

From: Biophysical characterization and solution structure of the cannulae-forming protein CanA from the hyperthermophilic archaeon Pyrodictium abyssi

Fig. 3

Amino acid sequence and secondary structure of CanA, CanB, and CanC. Amino acids removed in K1-CanA (grey), β-strands recognized in the 3D-NMR structure (blue), α-helices recognized in the 3D-NMR structure (orange), and β-strands or α-helices recognized by chemical shift analysis (boxed)10. Predicted helix α3 is only observed in one of the 10 lowest energy structures. CanA, CanB, and CanC sequences are taken from Mai8. Note that the N-terminal methionine M1 of CanA is introduced by the recombinant expression in E. coli and is not contained in the natural protein (and in the sequence presented by Kreitner et al.10).

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