Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity
TEM-1 β-lactamase evolved from ancestral enzymes that degraded a variety of β-lactam antibiotics with moderate efficiency and degrades β-lactam antibiotics with a strong preference for penicillins. Here authors developed a computational approach to rationally mold a protein flexibility profile on th...
Guardado en:
Autores principales: | Tushar Modi, Valeria A. Risso, Sergio Martinez-Rodriguez, Jose A. Gavira, Mubark D. Mebrat, Wade D. Van Horn, Jose M. Sanchez-Ruiz, S. Banu Ozkan |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/9f68b130500b474887f6a03663bb2f12 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family
por: Pablo Perez-Garcia, et al.
Publicado: (2021) -
Coenzyme Q at the Hinge of Health and Metabolic Diseases
por: Juan Diego Hernández-Camacho, et al.
Publicado: (2021) -
Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones.
por: Erik B Nordquist, et al.
Publicado: (2021) -
Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones
por: Erik B. Nordquist, et al.
Publicado: (2021) -
Design principles for shift current photovoltaics
por: Ashley M. Cook, et al.
Publicado: (2017)