Fig. 4: Structures of the 103-106 loop and interacting residues for CTX-M-14, CTX-M-14 N106S, CTX-M-15, TEM-1 apo-enzyme, and CTX-M-15 and TEM-1 in complex with BLIP. | Nature Communications

Fig. 4: Structures of the 103-106 loop and interacting residues for CTX-M-14, CTX-M-14 N106S, CTX-M-15, TEM-1 apo-enzyme, and CTX-M-15 and TEM-1 in complex with BLIP.

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

Fig. 4

a CTX-M-14 V103-N106 loop structure (pink). b CTX-M-15 V103-N106 loop structure (blue). c CTX-M-14 N106S mutant V103-S106 loop structure (orange). d TEM-1 V103-S106 loop structure (brown). e CTX-M-15 V103-N106 loop structure from the complex with BLIP (tan). f TEM-1 V103-S106 loop structure from a complex with BLIP (green). Oxygen and nitrogen atoms are shown in red and blue, respectively. Hydrogen bonds are shown as thin black lines as predicted by UCSF Chimera. The black arrow in each panel points to the position of the β-lactamase residue 104 carbonyl oxygen, which indicates the orientation of the 104–105 peptide bond. Note the flip in the peptide bond orientation between panels a and b versus c–f.

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