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...
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| Main Authors: | , , , , , , , |
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| Format: | article |
| Language: | EN |
| Published: |
Nature Portfolio
2017
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| Subjects: | |
| Online Access: | https://doaj.org/article/c491d2cfd1d84f3d8e686abfef8ef38c |
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