Figure 2: Mode of action of metallo-β-lactamases and binding mode of cyclic boronates. | Nature Communications

Figure 2: Mode of action of metallo-β-lactamases and binding mode of cyclic boronates.

From: Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates

Figure 2

(a) Outline mode of action of MBLs showing proposed intermediates. (b,c) Views from structures obtained by co-crystallization of 2 with BcII (b) and VIM-2 (Chain A) (c). Note the relative position of Trp87 is rotated by ∼180° compared with its position in structures of BcII and VIM-2 without inhibitor; in the case of VIM-2, Trp87 interacts with the cyclic boronate via a water molecule. (d) The overlay compares the binding modes of 2 and hydrolysed cefuroxime in complex with NDM-1 (PDB ID: 4RL2)). (e) Key active site interactions made by the cyclic boronates.

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