4U63
Crystal structure of a bacterial class III photolyase from Agrobacterium tumefaciens at 1.67A resolution
Summary for 4U63
| Entry DOI | 10.2210/pdb4u63/pdb |
| Descriptor | DNA photolyase, 5,10-METHENYL-6,7,8-TRIHYDROFOLIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | photolyase, dna repair, lyase, methenyltetrahydrofolate, cyclopyrimidine dimer, flavin, fad, flavoprotein, photoreduction, trp triade, double-stranded, dna damage, dna, ultraviolet rays, agrobacterium tumefaciens |
| Biological source | Agrobacterium tumefaciens |
| Total number of polymer chains | 1 |
| Total formula weight | 58748.56 |
| Authors | Scheerer, P.,Zhang, F.,Kalms, J.,von Stetten, D.,Krauss, N.,Oberpichler, I.,Lamparter, T. (deposition date: 2014-07-26, release date: 2015-03-25, Last modification date: 2023-12-20) |
| Primary citation | Scheerer, P.,Zhang, F.,Kalms, J.,von Stetten, D.,Krau, N.,Oberpichler, I.,Lamparter, T. The Class III Cyclobutane Pyrimidine Dimer Photolyase Structure Reveals a New Antenna Chromophore Binding Site and Alternative Photoreduction Pathways. J.Biol.Chem., 290:11504-11514, 2015 Cited by PubMed Abstract: Photolyases are proteins with an FAD chromophore that repair UV-induced pyrimidine dimers on the DNA in a light-dependent manner. The cyclobutane pyrimidine dimer class III photolyases are structurally unknown but closely related to plant cryptochromes, which serve as blue-light photoreceptors. Here we present the crystal structure of a class III photolyase termed photolyase-related protein A (PhrA) of Agrobacterium tumefaciens at 1.67-Å resolution. PhrA contains 5,10-methenyltetrahydrofolate (MTHF) as an antenna chromophore with a unique binding site and mode. Two Trp residues play pivotal roles for stabilizing MTHF by a double π-stacking sandwich. Plant cryptochrome I forms a pocket at the same site that could accommodate MTHF or a similar molecule. The PhrA structure and mutant studies showed that electrons flow during FAD photoreduction proceeds via two Trp triads. The structural studies on PhrA give a clearer picture on the evolutionary transition from photolyase to photoreceptor. PubMed: 25784552DOI: 10.1074/jbc.M115.637868 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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