Extended Data Fig. 2: NlpI blocks association of apo-rNDM-1 to Prc K477A, possibly by occupying the same binding site on the protease. | Nature Chemical Biology

Extended Data Fig. 2: NlpI blocks association of apo-rNDM-1 to Prc K477A, possibly by occupying the same binding site on the protease.

From: In-cell kinetic stability is an essential trait in metallo-β-lactamase evolution

Extended Data Fig. 2

a) SDS-PAGE analysis of SEC fractions from the left panel, corresponding to samples containing NlpI and apo-rNDM-1, with (bottom) or without (top) Prc K477A (two independent repetitions). b) Structural alignment of the Prc:NlpI complex (PDB 5WQL) and the proposed complex of Prc and apo-rNDM-1 (from Fig. 4b). NlpI and apo-rNDM-1 are shown as yellow and green ribbons, respectively, while Prc is shown in a magenta surface representation.

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