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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 3. The structure of SpnER2.

Figure 3

(a) SpnER2 is an MDR enzyme comprised of a substrate-binding domain (residues 190–307 and 448–501) and a nucleotide-binding subdomain (residues 308–447). (b) A superposition of SpnER2 (green) and ER from the porcine FAS (cyan) shows the different organization of the region surrounding βF, which usually forms the dimerization interface in MDR enzymes. (c) Conserved SpnER2 active site residues form specific interactions with a bound NADP+ molecule. Next to where the 4-pro-R hydride of NADPH would be positioned during the reduction reaction (indicated by *) are the lysine and aspartate implicated in catalysis as well as a tyrosine known to mediate stereoselectivity.