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. Author manuscript; available in PMC: 2010 Jun 2.
Published in final edited form as: Biochemistry. 2009 Jun 2;48(21):4476–4487. doi: 10.1021/bi8023509

Figure 5.

Figure 5

A. Residues F180 (green), close to the adenine moiety of FAD, and F272 (green), close to the isoalloxazine moiety of FAD (gray stick with N atoms = blue, O-atoms = red and P atoms = orange), were selected for mutagenesis to support the FAD binding area in MtmOIV (gold/blue ribbon). B. Residues L107, R204 and F89 (all in green) were chosen to support their involvement in the substrate (premithramycin B, gray stick with O-atoms = red) binding. The isoalloxazine moiety of FAD (gray stick with N-atoms = blue, O-atoms = red, P-atoms = orange) and the enzyme show in gold/blue ribbon. The results (Table 2) show that residues F89 and R204 possibly constrict the premithramycin B binding site, while the L107A mutation reduces substrate binding, and also FAD binding.