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- W4281651604 abstract "The resistance of bacteria to β-lactam antibiotics is primarily caused by the production of β-lactamases. Here, novel crystal structures of the native β-lactamase TEM-171 and two complexes with the widely used inhibitor tazobactam are presented, alongside complementary data from UV spectroscopy and fluorescence quenching. The six chemically identical β-lactamase molecules in the crystallographic asymmetric unit displayed different degrees of disorder. The tazobactam intermediate was covalently bound to the catalytic Ser70 in the trans-enamine configuration. While the conformation of tazobactam in the first complex resembled that in published β-lactamase-tazobactam structures, in the second complex, which was obtained after longer soaking of the native crystals in the inhibitor solution, a new and previously unreported tazobactam conformation was observed. It is proposed that the two complexes correspond to different stages along the deacylation path of the acyl-enzyme intermediate. The results provide a novel structural basis for the rational design of new β-lactamase inhibitors." @default.
- W4281651604 created "2022-06-13" @default.
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- W4281651604 date "2022-06-07" @default.
- W4281651604 modified "2023-10-15" @default.
- W4281651604 title "Crystal structures of the molecular class A β-lactamase TEM-171 and its complexes with tazobactam" @default.
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- W4281651604 doi "https://doi.org/10.1107/s2059798322004879" @default.
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