Fig. 3: PBP5 A485 has increased dynamics. | Nature Communications

Fig. 3: PBP5 A485 has increased dynamics.

From: Molecular basis of β-lactam antibiotic resistance of ESKAPE bacterium E. faecium Penicillin Binding Protein PBP5

Fig. 3

A 13C ILV side chain dynamics (T1ρ) comparison between PBP5T485 and PBP5A485 (delta T1ρ PBP5T485–T1ρ PBP5A485). Residues with increased dynamics have negative delta T1ρ values and are annotated. Error bars are based on repeat measurements and are often smaller than the symbols used. average ± std deviation. B 13C ILV side chain dynamics (T1ρ) comparison between PBP5T485:penG (1:8 saturation) and PBP5A485:penG (1:8 saturation) (delta T1ρ PBP5T485:penG–T1ρ PBP5A485:penG). Error bars are based on repeat measurements and are often smaller than the symbols used. average ± std deviation. Changes in T1ρ dynamics mapped on the PBP5 TP domain structure for C PBP5M485, D PBP5T485, and E PBP5A485. The catalytic S422 is shown as sticks, highlighted in yellow and labeled. The 485 residue is shown as orange sticks and labeled. Residues that experience dynamics are shown as sticks and colored in pink (C) or pink and magenta, with magenta indicating the residues that differ between M485 and T485 (D) or T485 and A485 (E). F PenG hydrolysis by PBP5A485 (green) and PBP5M485 (gray) following peak intensity via 1H NMR spectroscopy; Peak 1. Source data are provided as a Source Data file.

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