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- W1848996936 abstract "Abstract Coenzyme F 420 is a deazaflavin hydride carrier with a lower reduction potential than most flavins. In Mycobacterium tuberculosis ( Mtb ), F 420 plays an important role in activating PA‐824, an antituberculosis drug currently used in clinical trials. Although F 420 is important to Mtb redox metabolism, little is known about the enzymes that bind F 420 and the reactions that they catalyze. We have identified a novel F 420 ‐binding protein, Rv1155, which is annotated in the Mtb genome sequence as a putative flavin mononucleotide (FMN)‐binding protein. Using biophysical techniques, we have demonstrated that instead of binding FMN or other flavins, Rv1155 binds coenzyme F 420 . The crystal structure of the complex of Rv1155 and F 420 reveals one F 420 molecule bound to each monomer of the Rv1155 dimer. Structural, biophysical, and bioinformatic analyses of the Rv1155–F 420 complex provide clues about its role in the bacterium." @default.
- W1848996936 created "2016-06-24" @default.
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- W1848996936 date "2015-03-10" @default.
- W1848996936 modified "2023-10-13" @default.
- W1848996936 title "Molecular insights into the binding of coenzyme <scp>F<sub>420</sub></scp> to the conserved protein <scp>R</scp>v1155 from <scp><i>M</i></scp><i>ycobacterium tuberculosis</i>" @default.
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- W1848996936 doi "https://doi.org/10.1002/pro.2645" @default.
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