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. Author manuscript; available in PMC: 2010 Sep 2.
Published in final edited form as: Chem Biol. 2009 Jun 26;16(6):667–675. doi: 10.1016/j.chembiol.2009.04.011

Figure 1.

Figure 1

Figure 1

Comparison of the Three-dimensional Structures of the Acyltransferase Components of the Human Type I Cytosolic and Type II Mitochondrial Fatty Acid Synthase Systems The two structures were first superimposed and then displayed side-by-side for clarity. A: The structure of MAT includes the flanking aminoterminal (yellow) and carboxyterminal (grey) linkers that connect this domain to the adjacent domains in the megasynthase, β-ketoacyl synthase and dehydratase, respectively. B: The structure of the processed MT component of the mitochondrial fatty acid synthase with the mitochondrial targeting sequence removed. In both figures, the active site residues, histidine, serine and arginine are shown in green. C: Superimposition of the Active Sites of MAT (orange) and MT (grey). The region of MAT around Met499 was optimized as described in the Experimental Procedures. D: Primary and secondary structure alignments of the MAT and MT enzymes. The amino- and carboxyterminal linkers are colored yellow and grey, respectively and the three key active-site residues are marked with asterisks