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. Author manuscript; available in PMC: 2015 Aug 24.
Published in final edited form as: J Biol Chem. 2001 Mar 15;276(22):19141–19149. doi: 10.1074/jbc.M100329200

Fig. 6.

Fig. 6

A, the three-dimensional structure model of the wild type ALAS (monomeric). The superimposed three-dimensional structures of the wild type ALAS (yellow) and 7-amino-8-oxononanoate synthase (39) (Protein Data Base code 1BS0) (blue). B, the protein topology schematics (TOPS) of the predicted three-dimensional structures of wild type ALAS and circularly permuted ALAS variants. I, wild type ALAS, E16, L25, D472, and E491 variants. The two possible structural domains are shown. II, E13 and Q69 variants. III, N404 and N408 variants. The approximate positions of functional amino acid residues are indicated by arrows. The pointing triangles represent the β-strands “out of” or “into” the plane of the diagram, respectively; the circles represent α-helices (45). The /3-strands and the α-helices of the α/β structure central core are represented in solid black and patterned black, respectively.