Journal article

Publication year: 2012

Pages: 223-229

Journal: EMBO Reports

Volume number: 13

Issue number: 3

ISSN: 1469-221X

Open access status: Green

DOI Link: https://doi.org/10.1038/embor.2012.2

Publisher: Springer

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 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.

Harvard Citation style: Geisselbrecht, Y., Fruhwirth, S., Schroeder, C., Pierik, A., Klug, G. and Essen, L. (2012) CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors, EMBO Reports, 13(3), pp. 223-229. https://doi.org/10.1038/embor.2012.2

APA Citation style: Geisselbrecht, Y., Fruhwirth, S., Schroeder, C., Pierik, A., Klug, G., & Essen, L. (2012). CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors. EMBO Reports. 13(3), 223-229. https://doi.org/10.1038/embor.2012.2