6NVU
Crystal structure of TLA-1 extended spectrum Beta-lactamase in complex with Clavulanic Acid
Summary for 6NVU
| Entry DOI | 10.2210/pdb6nvu/pdb |
| Descriptor | Beta-lactamase, SULFATE ION, ACETATE ION, ... (9 entities in total) |
| Functional Keywords | lactamase, antibiotic, resistance, hydrolase, hydrolase-antibiotic complex, hydrolase/antibiotic |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 32186.24 |
| Authors | Rudino-Pinera, E.,Cifuentes-Castro, V.H.,Rodriguez-Almazan, C. (deposition date: 2019-02-05, release date: 2019-12-11, Last modification date: 2024-11-06) |
| Primary citation | Cifuentes-Castro, V.,Rodriguez-Almazan, C.,Silva-Sanchez, J.,Rudino-Pinera, E. The crystal structure of ESBL TLA-1 in complex with clavulanic acid reveals a second acylation site. Biochem.Biophys.Res.Commun., 522:545-551, 2020 Cited by PubMed Abstract: β-lactamases are the main molecules responsible for giving bacterial resistance against β-lactam antibiotics. The study of β-lactamases has allowed the development of antibiotics capable of inhibiting these enzymes. In this context, extended spectrum β-lactamase (ESBL) TLA-1 has spread in Escherichia coli and Enterobacter cloacae clinical isolates during the last 30 years in Mexico. In this research, the 3D structures of ESBL TLA-1 and TLA-1 S70G mutant, both ligand-free and in complex with clavulanic acid were determined by X-ray crystallography. Four clavulanic acid molecules were found in the structure of TLA-1, two of those were intermediaries of the acylation process and were localized covalently bound to two different amino acid residues, Ser70 and Ser237. The coordinates of TLA-1 in complex with clavulanic acid shows the existence of a second acylation site, additional to Ser70, which might be extendable to several members of the subclass A β-lactamases family. This is the first time that two serines involved in binding clavulanic acid has been reported and described to an atomic level. PubMed: 31780261DOI: 10.1016/j.bbrc.2019.11.138 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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