期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 18, 页码 11504-11514出版社
ELSEVIER
DOI: 10.1074/jbc.M115.637868
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资金
- Deutsche Forschungsgemeinschaft (DFG) [799/8-1, SFB 740-B6, SFB 1078-B6]
- China Scholarship Council
- Karlsruhe House of Young Scientists
- DFG Cluster of Excellence Unifying Concepts in Catalysis Research Field [D3/E3-1]
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-angstrom 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 pi-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.
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