Figure 5 | Scientific Reports

Figure 5

From: Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals Conformational Plasticity of Active Site

Figure 5

Flexibility of loop L1. In panel (A), superimposition of two chains of the BsCM_2-CGA structure shows the deviation in backbone position of residues corresponding to loop L1. Panel (B) depicts the conformational flexibility of loop L1 residues Arg45 and Phe46 in different structures (parentheses are corresponding residues in LmCM domain). Superimposition of BsCM_2-CGA chainB (orange), BsCM_2-CIT chainA (yellow) and LmCM domain (PDB ID: 3NVT) chainA (cyan) reveals the flipping of side chains of residues. In panel (C), superimposition of CM_2 domains has shown that loop L1 exists in different conformations. This backbone deviation and side chain flipping may participate in regulation of DAHPS activity by CM_2 domains. BsCM_2-CGA chainA (magenta), BsCM_2-CIT chainB (blue), E. coli P-protein’s CM domain (PDB ID: 1ECM) chainA (salmon) and MtCM (PDB ID: 2VKL) (raspberry) were used for structural analysis to assess the conformational flexibility of loop L1.

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