7CTQ
Peptidyl tryptophan dihydroxylase QhpG essential for tryptophylquinone cofactor biogenesis
Summary for 7CTQ
| Entry DOI | 10.2210/pdb7ctq/pdb |
| Descriptor | Peptidyl tryptophan dihydroxylase, FLAVIN-ADENINE DINUCLEOTIDE, HEXANE-1,6-DIOL, ... (5 entities in total) |
| Functional Keywords | fad-dependent monooxygenase, cofactor biogenesis, flavoprotein, cysteine tryptophylquinone, quinohemoprotein amine dehydrogenase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 2 |
| Total formula weight | 97342.07 |
| Authors | Oozeki, T.,Nakai, T.,Okajima, T. (deposition date: 2020-08-20, release date: 2021-02-17, Last modification date: 2024-03-27) |
| Primary citation | Oozeki, T.,Nakai, T.,Kozakai, K.,Okamoto, K.,Kuroda, S.,Kobayashi, K.,Tanizawa, K.,Okajima, T. Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor. Nat Commun, 12:933-933, 2021 Cited by PubMed Abstract: Bioconversion of peptidyl amino acids into enzyme cofactors is an important post-translational modification. Here, we report a flavoprotein, essential for biosynthesis of a protein-derived quinone cofactor, cysteine tryptophylquinone, contained in a widely distributed bacterial enzyme, quinohemoprotein amine dehydrogenase. The purified flavoprotein catalyzes the single-turnover dihydroxylation of the tryptophylquinone-precursor, tryptophan, in the protein substrate containing triple intra-peptidyl crosslinks that are pre-formed by a radical S-adenosylmethionine enzyme within the ternary complex of these proteins. Crystal structure of the peptidyl tryptophan dihydroxylase reveals a large pocket that may dock the protein substrate with the bound flavin adenine dinucleotide situated close to the precursor tryptophan. Based on the enzyme-protein substrate docking model, we propose a chemical reaction mechanism of peptidyl tryptophan dihydroxylation catalyzed by the flavoprotein monooxygenase. The diversity of the tryptophylquinone-generating systems suggests convergent evolution of the peptidyl tryptophan-derived cofactors in different proteins. PubMed: 33568660DOI: 10.1038/s41467-021-21200-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.978 Å) |
Structure validation
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