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...
| المؤلفون الرئيسيون: | , , , , , , , |
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| التنسيق: | مقال |
| اللغة: | English |
| منشور في: |
Nature Portfolio
2017-03-01
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| سلاسل: | Scientific Reports |
| الوصول للمادة أونلاين: | https://doi.org/10.1038/s41598-017-00402-6 |