The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes

Bifunctional FAD synthetases (FADSs) fold in two independent modules; The C-terminal riboflavin kinase (RFK) catalyzes the RFK activity, while the N-terminal FMN-adenylyltransferase (FMNAT) exhibits the FMNAT activity. The search for macromolecular interfaces in the Corynebacterium ammoniagenes FADS...

Descripción completa

Detalles Bibliográficos
Autores principales: Serrano, Ana, Sebastián, María, Arilla-Luna, Sonia, Baquedano, Silvia, Herguedas, Beatriz, Velázquez-Campoy, Adrián, Martínez-Júlvez, Marta, Medina, Milagros
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5428420/
https://www.ncbi.nlm.nih.gov/pubmed/28341845
http://dx.doi.org/10.1038/s41598-017-00402-6

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5428420/
https://www.ncbi.nlm.nih.gov/pubmed/28341845
http://dx.doi.org/10.1038/s41598-017-00402-6

Ejemplares similares