Close window
The EMBO Journal (2004) 23, 2745–2754, doi:10.1038/sj.emboj.7600298 Published online 1 July 2004 Figure 1 Structural basis for channelling mechanism of a fatty acid -oxidation multienzyme complex Momoyo Ishikawa, Daisuke Tsuchiya, Takuji Oyama, Yasuo Tsunaka and Kosuke Morikawa

Figure 1 -Oxidation spiral and structure of FOM complex. (A) Catalytic scheme of -oxidation spiral. (B) The subunit and domain organization of FOM compared with those of the hTFE complex, and the four monofunctional enzymes, rECH, hHACD, yKACT and zAACT. In the -subunit, the N-terminal domain is shown in brown, the -helical linker is yellow-green, the middle is green and the C-terminus is cyan, with the -subunit colored purple. The same color code is applied for all subsequent diagrams. Conserved catalytic residues are labelled using the single-letter code. (C) Symmetric Form I structure. Each subunit is distinguished by dark (1 and 1) and light coloring (2 and 2). Three ligands, NAD+ (dark blue), C8E5 (magenta) and Ac-CoA (red), are bound to each active site of the enzyme components. (D) Asymmetric Form II structure. The conversion of Form I to II is accompanied by large translations, as indicated by the bold arrows with lengths. It also generates the large difference (24 and 37 Å) in cleft sizes (top view).

previous | next

Privacy policy	Copyright © 2004 by the European Molecular Biology Organization