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

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

Abstract 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 ammoniag...

Täydet tiedot

Bibliografiset tiedot
Päätekijät: Ana Serrano, María Sebastián, Sonia Arilla-Luna, Silvia Baquedano, Beatriz Herguedas, Adrián Velázquez-Campoy, Marta Martínez-Júlvez, Milagros Medina
Aineistotyyppi: Artikkeli
Kieli:English
Julkaistu: Nature Portfolio 2017-03-01
Sarja:Scientific Reports
Linkit:https://doi.org/10.1038/s41598-017-00402-6

Internet

https://doi.org/10.1038/s41598-017-00402-6

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