2E0I
Crystal structure of archaeal photolyase from Sulfolobus tokodaii with two FAD molecules: Implication of a novel light-harvesting cofactor
Summary for 2E0I
| Entry DOI | 10.2210/pdb2e0i/pdb |
| Descriptor | 432aa long hypothetical deoxyribodipyrimidine photolyase, FLAVIN-ADENINE DINUCLEOTIDE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
| Functional Keywords | photolyase, fad, dna repair, sulfolobus tokodaii, lyase |
| Biological source | Sulfolobus tokodaii |
| Total number of polymer chains | 4 |
| Total formula weight | 217772.08 |
| Authors | Fujihashi, M.,Numoto, N.,Kobayashi, Y.,Mizushima, A.,Tsujimura, M.,Nakamura, A.,Kawarabayashi, Y.,Miki, K. (deposition date: 2006-10-10, release date: 2006-11-28, Last modification date: 2023-10-25) |
| Primary citation | Fujihashi, M.,Numoto, N.,Kobayashi, Y.,Mizushima, A.,Tsujimura, M.,Nakamura, A.,Kawarabayasi, Y.,Miki, K. Crystal Structure of Archaeal Photolyase from Sulfolobus tokodaii with Two FAD Molecules: Implication of a Novel Light-harvesting Cofactor J.Mol.Biol., 365:903-910, 2007 Cited by PubMed Abstract: UV exposure of DNA molecules induces serious DNA lesions. The cyclobutane pyrimidine dimer (CPD) photolyase repairs CPD-type - lesions by using the energy of visible light. Two chromophores for different roles have been found in this enzyme family; one catalyzes the CPD repair reaction and the other works as an antenna pigment that harvests photon energy. The catalytic cofactor of all known photolyases is FAD, whereas several light-harvesting cofactors are found. Currently, 5,10-methenyltetrahydrofolate (MTHF), 8-hydroxy-5-deaza-riboflavin (8-HDF) and FMN are the known light-harvesting cofactors, and some photolyases lack the chromophore. Three crystal structures of photolyases from Escherichia coli (Ec-photolyase), Anacystis nidulans (An-photolyase), and Thermus thermophilus (Tt-photolyase) have been determined; however, no archaeal photolyase structure is available. A similarity search of archaeal genomic data indicated the presence of a homologous gene, ST0889, on Sulfolobus tokodaii strain7. An enzymatic assay reveals that ST0889 encodes photolyase from S. tokodaii (St-photolyase). We have determined the crystal structure of the St-photolyase protein to confirm its structural features and to investigate the mechanism of the archaeal DNA repair system with light energy. The crystal structure of the St-photolyase is superimposed very well on the three known photolyases including the catalytic cofactor FAD. Surprisingly, another FAD molecule is found at the position of the light-harvesting cofactor. This second FAD molecule is well accommodated in the crystal structure, suggesting that FAD works as a novel light-harvesting cofactor of photolyase. In addition, two of the four CPD recognition residues in the crystal structure of An-photolyase are not found in St-photolyase, which might utilize a different mechanism to recognize the CPD from that of An-photolyase. PubMed: 17107688DOI: 10.1016/j.jmb.2006.10.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
