2j07 | pdb_00002j07
From Proteopedia
THERMUS DNA PHOTOLYASE WITH 8-HDF ANTENNA CHROMOPHORE
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedX-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
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