Volume 103, Issue 5, Pages (September 2012)

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Volume 103, Issue 5, Pages 1037-1044 (September 2012) Rigidifying Acyl Carrier Protein Domain in Iterative Type I PKS CalE8 Does Not Affect Its Function Jackwee Lim, Huihua Sun, Jing-Song Fan, Iman Fahim Hameed, Julien Lescar, Zhao-Xun Liang, Daiwen Yang Biophysical Journal Volume 103, Issue 5, Pages 1037-1044 (September 2012) DOI: 10.1016/j.bpj.2012.08.006 Copyright © 2012 Biophysical Society Terms and Conditions

Figure 1 (a) Domain organization of CalE8 and ribbon structure of meACP, with S971, A938C, and E1009C highlighted. (b) Thermal denaturation profiles of meACP and its mutant monitored at 222 nm by CD. (c) CD profiles of meACP and its mutant with and without 1.7 mM TCEP at 25°C. Biophysical Journal 2012 103, 1037-1044DOI: (10.1016/j.bpj.2012.08.006) Copyright © 2012 Biophysical Society Terms and Conditions

Figure 2 Sequential- and medium-range NOE patterns of the meACP mutant. The NOE intensities are represented by the thickness of the solid bars. The secondary structure elements of the WT protein are indicated at the top of the sequence. Biophysical Journal 2012 103, 1037-1044DOI: (10.1016/j.bpj.2012.08.006) Copyright © 2012 Biophysical Society Terms and Conditions

Figure 3 Comparison of 15N-{1H} NOEs for WT meACP (•) and its mutant (○). The locations of two cysteine residues in the mutant are indicated by arrows on the secondary structure diagram. Biophysical Journal 2012 103, 1037-1044DOI: (10.1016/j.bpj.2012.08.006) Copyright © 2012 Biophysical Society Terms and Conditions

Figure 4 Representative relaxation dispersion profiles of meACP (a–e) and comparison of experimental (δmi) and random coil (δrandom) 15N chemical shifts of the invisible minor form (f). The experimental data recorded by 500 and 800 MHz NMR are indicated by ○ and ∗, respectively, and solid lines are fitting curves in panels a–e. Biophysical Journal 2012 103, 1037-1044DOI: (10.1016/j.bpj.2012.08.006) Copyright © 2012 Biophysical Society Terms and Conditions

Figure 5 Comparison of P factors for WT (bar) and mutant (∗) meACP. P factors were calculated from amide hydrogen exchange rates (kex) and random coil exchange rates. For the WT meACP, kex values were previously measured at pH 6.9 and 7.5 using an exchange spectroscopy (EXSY) scheme. For the mutant, kex values were obtained using either the EXSY scheme or the H-D exchange method. When P < 100 or log(P) < 2, kex could be measured using the EXSY scheme. When P > 1000 or log(P) > 3, kex could be measured using the H-D exchange scheme. When 100 < P < 1000, kex could not be measured by these two methods. The locations of two cysteine residues in the mutant are indicated by arrows on the secondary structure diagram. Biophysical Journal 2012 103, 1037-1044DOI: (10.1016/j.bpj.2012.08.006) Copyright © 2012 Biophysical Society Terms and Conditions

Figure 6 Enzymatic activity of CalE8 and the double mutant. (A) Absorption spectra of the WT and mutant CalE8 expressed from E. coli. (B and C) Comparison of the enzymatic activity of CalE8 and the double mutant under (B) oxidizing and (C) reducing conditions. Biophysical Journal 2012 103, 1037-1044DOI: (10.1016/j.bpj.2012.08.006) Copyright © 2012 Biophysical Society Terms and Conditions