6PUQ
1.56 A crystal structure of flavodoxin-like domain of Schizosaccharomyces japonicus putative tRNAPhe 4-demethylwyosine synthase Tyw1 in complex with FMN
Summary for 6PUQ
Entry DOI | 10.2210/pdb6puq/pdb |
Descriptor | Wybutosine biosynthesis protein Tyw1, FLAVIN MONONUCLEOTIDE, MAGNESIUM ION, ... (6 entities in total) |
Functional Keywords | trna, hypermodification, wyosine, flavoprotein |
Biological source | Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast) |
Total number of polymer chains | 1 |
Total formula weight | 25515.41 |
Authors | Sjekloca, L.,Ferre-D'Amare, A.R. (deposition date: 2019-07-18, release date: 2020-07-22, Last modification date: 2024-05-22) |
Primary citation | Sjekloca, L.,Ferre-D'Amare, A.R. Biochemical and structural characterization of the flavodoxin-like domain of the Schizosaccharomyces japonicus putative tRNAPhe 4-demethylwyosine synthase Tyw1 in complex with FMN. MicroPubl Biol, 2022:-, 2022 Cited by PubMed Abstract: The S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1 catalyzes biosynthesis of 4-demethylwyosine (imG-14), the precursor for wyosine, the hypermodified guanine-derived nucleotide present at position 37 of phenylalanine tRNAs of archaea and eukarya. Eukaryotic TYW1 enzymes contain N-terminal flavodoxin-like and C-terminal radical-SAM domains. We determined co-crystal structures of the flavodoxin-like domain of the putative Tyw1 from in complex with flavin mononucleotide (FMN), exploiting an unexpected anomalous scatterer present in the recombinant protein. Our results show how eukaryotic TYW1 enzymes bind the coenzyme FMN and will help further elucidation of the structural enzymology of 4-demethylwyosine synthesis. PubMed: 35693892DOI: 10.17912/micropub.biology.000570 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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