Figure 7 | Scientific Reports

Figure 7

From: Structural and functional characterization of M. tuberculosis sedoheptulose- 7-phosphate isomerase, a critical enzyme involved in lipopolysaccharide biosynthetic pathway

Figure 7

(A) Dynamic simulation on apo MtbGmhA tetramer. The simulated MtbGmhA tetramer (Green) is superposed on starting structure (Grey). (B) Plot showing the B-factor (Y-axis) and residue number (X-axis) of simulated MtbGmhA tetramer. (C) Dynamic simulation on MtbGmhA + D-sedoheptulose 7-phosphate tetramer. The simulated MtbGmhA + D-sedoheptulose 7-phosphate tetramer (red) is superposed on starting structure (grey). (D) The B-factor (Y-axis) and residue number (X-axis) of simulated MtbGmhA + D-sedoheptulose 7-phosphate tetramer. (E) Dynamic simulation on MtbGmhA + D-sedoheptulose 7-phosphate + Zn2+ tetramer. The simulated complex (blue) is superposed on starting structure (grey). (F) The B-factor (Y-axis) and residue number (X-axis) of simulated MtbGmhA + D-sedoheptulose 7-phosphate + Zn2+ tetramer. (G) The plot showing the backbone RMSD ~ time for apo, D-sedoheptulose 7-phosphate bound and D-sedoheptulose 7-phosphate + Zn2+ bound MtbGmhA tetramer. (H) The plot showing the radius of gyration (Rg) ~ time, which showed the changes in degree of compactness of MtbGmhA tetramer after D-sedoheptulose 7-phosphate and Zn2+ binding.

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