Structural highlights
Function
[PHR_THET8] Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
X-ray crystallographic and functional analysis of the class I DNA photolyase from Thermus thermophilus revealed the binding of flavin mononucleotide (FMN) as an antenna chromophore. The binding mode of FMN closely coincides with the binding of a deazaflavin-like chromophore in the related class I DNA photolyase from Anacystis nidulans. Compared to the R46E mutant, which lacks a conserved arginine in the binding site for the antenna chromophore, the FMN-comprising holophotolyase exhibits an eightfold higher activity at 450 nm. The facile incorporation of the flavin cofactors 8-hydroxy-deazariboflavin and 8-iodo-8-demethyl-riboflavin into the binding site for the antenna chromophore paves the way for wavelength-tuning of the activity spectra of DNA photolyases by using synthetic flavins.
Natural and non-natural antenna chromophores in the DNA photolyase from Thermus thermophilus.,Klar T, Kaiser G, Hennecke U, Carell T, Batschauer A, Essen LO Chembiochem. 2006 Nov;7(11):1798-806. PMID:17051659[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Klar T, Kaiser G, Hennecke U, Carell T, Batschauer A, Essen LO. Natural and non-natural antenna chromophores in the DNA photolyase from Thermus thermophilus. Chembiochem. 2006 Nov;7(11):1798-806. PMID:17051659 doi:10.1002/cbic.200600206
