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Structural basis for the ligand promiscuity of the neofunctionalized, carotenoid-binding fasciclin domain protein AstaPстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Kornilov Fedor D., Slonimskiy Yury B., Lunegova Daria A., Egorkin Nikita A., Savitskaya Anna G., Kleymenov Sergey Yu, Maksimov Eugene G., Goncharuk Sergey A., Mineev Konstantin S., Sluchanko Nikolai N.
- Журнал: Communications Biology
- Том: 6
- Номер: 1
- Год издания: 2023
- Издательство: Springer Nature
- Местоположение издательства: Switzerland
- DOI: 10.1038/s42003-023-04832-z
- Аннотация: Fasciclins (FAS1) are ancient adhesion protein domains with no common small ligand binding reported. A unique microalgal FAS1-containing astaxanthin (AXT)-binding protein (AstaP) binds a broad repertoire of carotenoids by a largely unknown mechanism. Here, we explain the ligand promiscuity of AstaP-orange1 (AstaPo1) by determining its NMR structure in complex with AXT and validating this structure by SAXS, calorimetry, optical spectroscopy and mutagenesis. α1-α2 helices of the AstaPo1 FAS1 domain embrace the carotenoid polyene like a jaw, forming a hydrophobic tunnel, too short to cap the AXT β-ionone rings and dictate specificity. AXT-contacting AstaPo1 residues exhibit different conservation in AstaPs with the tentative carotenoid-binding function and in FAS1 proteins generally, which supports the idea of AstaP neofunctionalization within green algae. Intriguingly, a cyanobacterial homolog with a similar domain structure cannot bind carotenoids under identical conditions. These structure-activity relationships provide the first step towards the sequence-based prediction of the carotenoid-binding FAS1 members.
- Добавил в систему: Максимов Евгений Георгиевич