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Figure 4
(a) The different conformations the inhibitor 4,7-dioxosebacic acid adopts when binding to different ALADs are shown. The conformation of the inhibitor bound to the E. coli enzyme is shown in pink, while that of the yeast enzyme is shown in purple, with the conformation of the inhibitor bound to C. vibrioforme ALAD shown in green. (b) The interactions of 4,7-dioxosebacic acid from the three structures with the residues making up the A-site (the colouring scheme remains the same). Lys222 from the C. vibrioforme structure is replaced by an arginine residue in both the E. coli and yeast ALADs.

Journal logoBIOLOGICAL
ISSN: 1399-0047
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