3CVV

Drosophila melanogaster (6-4) photolyase bound to ds DNA with a T-T (6-4) photolesion and F0 cofactor

Summary for 3CVV

• Entry DOI: 10.2210/pdb3cvv/pdb
• Related: 3CVU 3CVW 3CVX 3CVY
• Descriptor: DNA (5'-D(*DAP*DCP*DAP*DGP*DCP*DGP*DGP*(64T)P*(5PY)P*DGP*DCP*DAP*DGP*DGP*DT)-3'), DNA (5'-D(*DTP*DAP*DCP*DCP*DTP*DGP*DCP*DAP*DAP*DCP*DCP*DGP*DCP*DTP*DG)-3'), RE11660p, ... (7 entities in total)
• Functional Keywords: dna repair, lyase-dna complex, lyase/dna
• Biological source: Drosophila melanogaster
• Total number of polymer chains: 3
• Total formula weight: 73489.27

Authors

Glas, A.F.,Maul, M.J.,Cryle, M.J.,Barends, T.R.M.,Schneider, S.,Kaya, E.,Schlichting, I.,Carell, T. (deposition date: 2008-04-20, release date: 2009-06-16, Last modification date: 2024-02-21)

Primary citation

Glas, A.F.,Maul, M.J.,Cryle, M.,Barends, T.R.,Schneider, S.,Kaya, E.,Schlichting, I.,Carell, T.
The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes.
Proc.Natl.Acad.Sci.USA, 106:11540-11545, 2009

PubMed Abstract: Archae possess unique biochemical systems quite distinct from the pathways present in eukaryotes and eubacteria. 7,8-Dimethyl-8-hydroxy-5deazaflavin (F(0)) and F(420) are unique deazaflavin-containing coenzyme and methanogenic signature molecules, essential for a variety of biochemical transformations associated with methane biosynthesis and light-dependent DNA repair. The deazaflavin cofactor system functions during methane biosynthesis as a low-potential hydrid shuttle F(420)/F(420)H(2). In DNA photolyase repair proteins, the deazaflavin cofactor is in the deprotonated state active as a light-collecting energy transfer pigment. As such, it converts blue sunlight into energy used by the proteins to drive an essential repair process. Analysis of a eukaryotic (6-4) DNA photolyase from Drosophila melanogaster revealed a binding pocket, which tightly binds F(0). Residues in the pocket activate the cofactor by deprotonation so that light absorption and energy transfer are switched on. The crystal structure of F(0) in complex with the D. melanogaster protein shows the atomic details of F(0) binding and activation, allowing characterization of the residues involved in F(0) activation. The results show that the F(0)/F(420) coenzyme system, so far believed to be strictly limited to the archael kingdom of life, is far more widespread than anticipated. Analysis of a D. melanogaster extract and of a DNA photolyase from the primitive eukaryote Ostreococcus tauri provided direct proof for the presence of the F(0) cofactor also in higher eukaryotes.

PubMed: 19570997
DOI: 10.1073/pnas.0812665106

Experimental method

X-RAY DIFFRACTION (2.1 Å)