期刊
EMBO REPORTS
卷 13, 期 3, 页码 223-229出版社
WILEY
DOI: 10.1038/embor.2012.2
关键词
CryPro; cryptochrome; iron-sulphur cluster; lumazine-binding protein; Rhodobacter sphaeroides
资金
- Volkswagen-Stiftung
- Deutsche Forschungsgemeinschaft
Cryptochromes and photolyases are structurally related but have different biological functions in signalling and DNA repair. Proteobacteria and cyanobacteria harbour a new class of cryptochromes, called CryPro. We have solved the 2.7 angstrom structure of one of its members, cryptochrome B from Rhodobacter sphaeroides, which is a regulator of photosynthesis gene expression. The structure reveals that, in addition to the photolyase-like fold, CryB contains two cofactors only conserved in the CryPro subfamily: 6,7-dimethyl-8-ribityl-lumazine in the antenna-binding domain and a [4Fe-4S] cluster within the catalytic domain. The latter closely resembles the iron-sulphur cluster harbouring the large primase subunit PriL, indicating that PriL is evolutionarily related to the CryPro class of cryptochromes.
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