| Literature DB >> 22290493 |
Yann Geisselbrecht1, Sebastian Frühwirth, Claudia Schroeder, Antonio J Pierik, Gabriele Klug, Lars-Oliver Essen.
Abstract
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 Å 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.Entities:
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Year: 2012 PMID: 22290493 PMCID: PMC3323124 DOI: 10.1038/embor.2012.2
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807