Fig. 1: Structure representation of BLIP binding to TEM-1 and CTX-M-15 β-lactamases. | Nature Communications

Fig. 1: Structure representation of BLIP binding to TEM-1 and CTX-M-15 β-lactamases.

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

Fig. 1

a Ribbon diagram of BLIP (gray) binding to TEM-1 β-lactamase (green, surface) (PDB id: 1JTG). b Structure of BLIP (gray) binding to TEM-1 β-lactamase (green) superimposed with BLIP (blue) binding to CTX-M-15 β-lactamase (tan). c Structure of BLIP (blue) binding to CTX-M-15 β-lactamase (tan). Key BLIP residues that interact with CTX-M-15 are shown in ball and stick (green) and labeled. The 103–106 loop region of CTX-M-15 is highlighted in pink. d BLIP/CTX-M-15 active site region rotated clockwise 90° from view in c.

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