5o86 | pdb_00005o86

Mutant of claas II CPD photolyase from Methanosarcina mazei - W388F

spinqualitylabelsall models 5o86, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o86 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, GOL, SO4 Activity: Deoxyribodipyrimidine photo-lyase, with EC number 4.1.99.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. This article is protected by copyright. All rights reserved. Nicotinamide Adenine Dinucleotides Arrest Photoreduction of Class II DNA Photolyases in FADH State.,Ignatz E, Geisselbrecht Y, Kiontke S, Essen LO Photochem Photobiol. 2017 Aug 31. doi: 10.1111/php.12834. PMID:28858395 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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