Summary for 7QOR
| Entry DOI | 10.2210/pdb7qor/pdb |
| Descriptor | Beta-lactamase TEM, 1,2-ETHANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total) |
| Functional Keywords | beta-lactamase, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 6 |
| Total formula weight | 174221.61 |
| Authors | Hakanpaa, J.,Petrova, T.,Samygina, V.R.,Chojnowski, G.,Lamzin, V.,Egorov, A.M. (deposition date: 2021-12-28, release date: 2022-07-13, Last modification date: 2024-01-31) |
| Primary citation | Grigorenko, V.G.,Petrova, T.E.,Carolan, C.,Rubtsova, M.Y.,Uporov, I.V.,Pereira, J.,Chojnowski, G.,Samygina, V.R.,Lamzin, V.S.,Egorov, A.M. Crystal structures of the molecular class A beta-lactamase TEM-171 and its complexes with tazobactam. Acta Crystallogr D Struct Biol, 78:825-834, 2022 Cited by PubMed 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. PubMed: 35775982DOI: 10.1107/S2059798322004879 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.999 Å) |
Structure validation
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