5O8D

Mutant of class II CPD photolyase from Methanosarcina mazei - Y345F

5O8D の概要

• エントリーDOI: 10.2210/pdb5o8d/pdb
• 分子名称: Deoxyribodipyrimidine photolyase, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: photoreduction, lyase
• 由来する生物種: Methanosarcina mazei Go1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57090.07

構造登録者

Ignatz, E.,Essen, L.-O. (登録日: 2017-06-13, 公開日: 2017-09-13, 最終更新日: 2024-05-08)

主引用文献

Ignatz, E.,Geisselbrecht, Y.,Kiontke, S.,Essen, L.O.
Nicotinamide Adenine Dinucleotides Arrest Photoreduction of Class II DNA Photolyases in FADH ̇ State.
Photochem. Photobiol., 94:81-87, 2018

PubMed Abstract: All light-sensitive members of the photolyase/cryptochrome family rely on FAD as catalytic cofactor. Its activity is regulated by photoreduction, a light-triggered electron transfer process from a conserved tryptophan triad to the flavin. The stability of the reduced flavin depends on available external electron donors and oxygen. In this study, we show for the class II photolyase of Methanosarcina mazei, MmCPDII, that it utilizes physiologically relevant redox cofactors NADH and NADPH for the formation of the semiquinoid FAD in a light-dependent reaction. Using redox-inert variants MmCPDII/W388F and MmCPDII/W360F, we demonstrate that photoreduction by NADH and NADPH requires the class II-specific tryptophan cascade of MmCPDII. Finally, we confirmed that mutations in the tryptophan cascade can be introduced without any substantial structural disturbances by analyzing crystal structures of MmCPDII/W388F, MmCPDII/W360F and MmCPDII/Y345F.

PubMed: 28858395
DOI: 10.1111/php.12834

実験手法

X-RAY DIFFRACTION (2 Å)