Structural highlights
Publication Abstract from PubMed
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 A 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.
CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors.,Geisselbrecht Y, Fruhwirth S, Schroeder C, Pierik AJ, Klug G, Essen LO EMBO Rep. 2012 Jan 31. doi: 10.1038/embor.2012.2. PMID:22290493[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Geisselbrecht Y, Fruhwirth S, Schroeder C, Pierik AJ, Klug G, Essen LO. CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors. EMBO Rep. 2012 Jan 31. doi: 10.1038/embor.2012.2. PMID:22290493 doi:10.1038/embor.2012.2
