|
|
| Line 1: |
Line 1: |
| [[Image:2e0i.gif|left|200px]] | | {{Seed}} |
| | [[Image:2e0i.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2e0i| PDB=2e0i | SCENE= }} | | {{STRUCTURE_2e0i| PDB=2e0i | SCENE= }} |
|
| |
|
| '''Crystal structure of archaeal photolyase from Sulfolobus tokodaii with two FAD molecules: Implication of a novel light-harvesting cofactor'''
| | ===Crystal structure of archaeal photolyase from Sulfolobus tokodaii with two FAD molecules: Implication of a novel light-harvesting cofactor=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17107688}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17107688 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_17107688}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 36: |
Line 40: |
| [[Category: Photolyase]] | | [[Category: Photolyase]] |
| [[Category: Sulfolobus tokodaii]] | | [[Category: Sulfolobus tokodaii]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:42:33 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:55:22 2008'' |
