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Crystal structure of AmpC BER and molecular docking lead to the discovery of broad inhibition activities of halisulfates against β-lactamases
AmpC BER is an extended-spectrum (ES) class C β-lactamase with a two-amino-acid insertion in the H10 helix region located at the boundary of the active site compared with its narrow spectrum progenitor. The crystal structure of the wild-type AmpC BER revealed that the insertion widens the active sit...
| Autores principales: | , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Research Network of Computational and Structural Biotechnology
2020
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773887/ https://www.ncbi.nlm.nih.gov/pubmed/33425247 http://dx.doi.org/10.1016/j.csbj.2020.12.015 |