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. Author manuscript; available in PMC: 2013 Jan 1.
Published in final edited form as: Nat Chem Biol. 2012 May 27;8(7):615–621. doi: 10.1038/nchembio.964

Figure 2. KR+ER architecture.

Figure 2

(a) The crystal structure of Spn(KR+ER)2 shows the interface between the structural and catalytic subdomains of its KR (KRs and KRc) and ER, which is mostly formed by hydrophilic residues. The N- and C-terminal linkers help mediate the interface, Trp506 inserting into a hydrophobic pocket of KRc. (b) The structure of the porcine FAS shows a very different interface between its KR and ER and how ER dimerizes across the twofold axis of the FAS. The C-terminal linker is longer than that of Spn(KR+ER)2 (29 vs. 8 residues). (c) SAXS data were obtained for Spn(KR+ER)2 and compared to the theoretical curves predicted by the program CRYSOL for a model generated from the Spn(KR+ER)2 crystal structure (red curve), and for a model generated by superposing SpnKR2 and SpnER2 on the KR and ER from the porcine FAS (blue curve). (d) An ab initio molecular envelope was generated from the SAXS curve (by the program DAMMIF), which was much better fit by the model generated from the Spn(KR+ER)2 crystal structure (using the program SUPCOMB).