7CTQ

Peptidyl tryptophan dihydroxylase QhpG essential for tryptophylquinone cofactor biogenesis

7CTQ の概要

• エントリーDOI: 10.2210/pdb7ctq/pdb
• 分子名称: Peptidyl tryptophan dihydroxylase, FLAVIN-ADENINE DINUCLEOTIDE, HEXANE-1,6-DIOL, ... (5 entities in total)
• 機能のキーワード: fad-dependent monooxygenase, cofactor biogenesis, flavoprotein, cysteine tryptophylquinone, quinohemoprotein amine dehydrogenase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97342.07

構造登録者

Oozeki, T.,Nakai, T.,Okajima, T. (登録日: 2020-08-20, 公開日: 2021-02-17, 最終更新日: 2024-03-27)

主引用文献

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

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: 33568660
DOI: 10.1038/s41467-021-21200-9

実験手法

X-RAY DIFFRACTION (1.978 Å)