4qvb
Mycobacterium tuberculosis protein Rv1155 in complex with co-enzyme F420Mycobacterium tuberculosis protein Rv1155 in complex with co-enzyme F420
Structural highlights
FunctionF420R_MYCTU F420H(2)-dependent reductase able to catalyze the reduction of biliverdin-IXalpha to bilirubin-IXalpha in vitro. However, kinetic parameters show that it is less efficient than the biliverdin reductase Rv2074 and suggest biliverdin-IXalpha is unlikely to be the native substrate of Rv1155, which probably catalyzes the reduction of an alternative molecule in vivo (PubMed:27364382). Binds coenzyme F420, but does not bind FMN or other flavins (PubMed:25644473). Cannot use pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate, pyridoxal 5'-phosphate (PLP), the anti-tuberculosis drug PA-824 or aflatoxin analogs as substrates (PubMed:25644473).[1] [2] Publication Abstract from PubMedCoenzyme F420 is a deazaflavin hydride carrier with a lower reduction potential than most flavins. In Mycobacterium tuberculosis (Mtb), F420 plays an important role in activating PA-824, an anti-tuberculosis drug currently in clinical trials. Although F420 is important to Mtb redox metabolism, little is known about the enzymes that bind F420 and the reactions that they catalyze. We have identified a novel F420 -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 F420 . The crystal structure of the complex of Rv1155 and F420 reveals one F420 molecule bound to each monomer of the Rv1155 dimer. Structural, biophysical, and bioinformatic analyses of the Rv1155-F420 complex provide clues about its role in the bacterium. This article is protected by copyright. All rights reserved. Molecular insights into the binding of coenzyme F to the conserved protein Rv1155 from Mycobacterium tuberculosis.,Mashalidis EH, Gittis AG, Tomczak A, Abell C, Barry CE 3rd, Garboczi DN Protein Sci. 2015 Jan 31. doi: 10.1002/pro.2645. PMID:25644473[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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