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CryB from Rhodobacter sphaeroides : a unique class of cryptochromes with new cofactors
Author(s) -
Geisselbrecht Yann,
Frühwirth Sebastian,
Schroeder Claudia,
Pierik Antonio J,
Klug Gabriele,
Essen LarsOliver
Publication year - 2012
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2012.2
Subject(s) - cryptochrome , photolyase , rhodobacter sphaeroides , cofactor , subfamily , biology , biochemistry , photosynthesis , gene , dna repair , enzyme , circadian clock
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.