Fig. 7: Molecular dynamics simulations of CTX-M apo-enzymes and CTX-M/BLIP complexes. | Nature Communications

Fig. 7: Molecular dynamics simulations of CTX-M apo-enzymes and CTX-M/BLIP complexes.

From: An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M β-lactamase drug-resistance enzymes

Fig. 7

a The RMSD of CTX-M-14 loop 103-106 backbone throughout the 100 ns MD simulations. Six replicate simulations are shown. b The RMSD of CTX-M-15 loop 103-106 backbone for six replicate 100 ns MD simulations. c The RMSD of CTX-M-14 N106S loop 103-106 backbone for six replicate 100 ns MD simulations. d The dynamic change of distance (nm) between CTX-M-14 Tyr105 backbone nitrogen and BLIP Glu73 side chain carboxylate oxygen atom throughout three replicate 100 ns MD simulations of a modeled structure of CTX-M-14 in complex with BLIP. e The dynamic change of distance (nm) between CTX-M-15 Tyr105 backbone nitrogen and BLIP Glu73 side chain carboxylate oxygen atom throughout three replicate 100 ns MD simulations using the CTX-M-15/BLIP X-ray structure. f The dynamic change of distance (nm) between CTX-M-14 N106S Tyr105 backbone nitrogen and BLIP Glu73 side chain carboxylate oxygen atom throughout three replicate 100 ns MD simulations of a modeled structure of CTX-M-14 N106S in complex with BLIP.

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