Control of Bacterial Iron Transport by Regulatory Proteins

Abstract

Cover figure: Structure of the pig heart mitochondrial aconitase (see Fig. 7.5, p. 185): The protei n secondary structur e is represented by yellow coils for helices and red ribbon s for strands withi n the ß sheets. The N terminu s is at the lower righ t and the C terminu s at the upper right. The [Fe-4S ] cluster and bound isocitrate (stick models) are in the center. The yellow (S) and red (Fe) spheres of the cluster and black (C) and red (0) spheres of isocitrate are shown. Four polypeptid e domain s are best seen in the figur e by viewin g their bundles of red ß strands. Large blue spheres marked wit h arrow s at the left represent the location of Gly 108 (bottom) and Leu 590 (top) which , based on sequence alignment , represent the approximat e locations of the phosphorylatio n sites of IRP-1 at Serl38 and Ser711. For more information , see Fig. 7.5 on p. 185, whic h includes a schematic view of the IRE RNA molecule positioned next to aconitase. The cover figur e was supplie d bv C. D. Stout (Scripps Institute). The reader is referred to Chapter 7 for futher information .