2E0I

Crystal structure of archaeal photolyase from Sulfolobus tokodaii with two FAD molecules: Implication of a novel light-harvesting cofactor

2E0I の概要

• エントリーDOI: 10.2210/pdb2e0i/pdb
• 分子名称: 432aa long hypothetical deoxyribodipyrimidine photolyase, FLAVIN-ADENINE DINUCLEOTIDE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: photolyase, fad, dna repair, sulfolobus tokodaii, lyase
• 由来する生物種: Sulfolobus tokodaii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 217772.08

構造登録者

Fujihashi, M.,Numoto, N.,Kobayashi, Y.,Mizushima, A.,Tsujimura, M.,Nakamura, A.,Kawarabayashi, Y.,Miki, K. (登録日: 2006-10-10, 公開日: 2006-11-28, 最終更新日: 2024-11-06)

主引用文献

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

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: 17107688
DOI: 10.1016/j.jmb.2006.10.012

実験手法

X-RAY DIFFRACTION (2.8 Å)