5O8E

Mutant of class II CPD photolyase from Methanosarcina mazei

Summary for 5O8E

• Entry DOI: 10.2210/pdb5o8e/pdb
• Descriptor: Deoxyribodipyrimidine photolyase, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• Functional Keywords: photoreduction, lyase
• Biological source: Methanosarcina mazei Go1
• Total number of polymer chains: 1
• Total formula weight: 57067.04

Authors

Ignatz, E.,Geisselbrecht, Y.,Essen, L.-O. (deposition date: 2017-06-13, release date: 2017-09-13, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)