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...

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Detalles Bibliográficos
Autores principales: Jeong, Bo-Gyeong, Na, Jung-Hyun, Bae, Da-Woon, Park, Soo-Bong, Lee, Hyi-Seung, Cha, Sun-Shin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2020
Materias:
Research Article
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

Internet

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

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