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Molecular insights into the binding of coenzyme F420 to the conserved protein Rv1155 from M ycobacterium tuberculosis.
- Source :
- Protein Science: A Publication of the Protein Society; May2015, Vol. 24 Issue 5, p729-740, 12p
- Publication Year :
- 2015
-
Abstract
- Coenzyme F<subscript>420</subscript> is a deazaflavin hydride carrier with a lower reduction potential than most flavins. In Mycobacterium tuberculosis ( Mtb), F<subscript>420</subscript> plays an important role in activating PA-824, an antituberculosis drug currently used in clinical trials. Although F<subscript>420</subscript> is important to Mtb redox metabolism, little is known about the enzymes that bind F<subscript>420</subscript> and the reactions that they catalyze. We have identified a novel F<subscript>420</subscript>-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<subscript>420</subscript>. The crystal structure of the complex of Rv1155 and F<subscript>420</subscript> reveals one F<subscript>420</subscript> molecule bound to each monomer of the Rv1155 dimer. Structural, biophysical, and bioinformatic analyses of the Rv1155-F<subscript>420</subscript> complex provide clues about its role in the bacterium. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09618368
- Volume :
- 24
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Protein Science: A Publication of the Protein Society
- Publication Type :
- Academic Journal
- Accession number :
- 102270238
- Full Text :
- https://doi.org/10.1002/pro.2645