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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / classification
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Bacterial Proteins / genetics
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Binding Sites
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Cryptochromes / chemistry*
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Cryptochromes / classification
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Cryptochromes / genetics
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Crystallography, X-Ray
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Deoxyribodipyrimidine Photo-Lyase / chemistry
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Deoxyribodipyrimidine Photo-Lyase / genetics
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Ferrocyanides / chemistry
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Flavin-Adenine Dinucleotide / chemistry
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Hydrogen Bonding
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Models, Molecular
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Molecular Sequence Data
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Oxidation-Reduction
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Phylogeny
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Protein Binding
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Protein Structure, Tertiary
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Pteridines / chemistry
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Rhodobacter sphaeroides / chemistry*
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Rhodobacter sphaeroides / genetics
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Sequence Alignment
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Static Electricity
Substances
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Bacterial Proteins
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Cryptochromes
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Ferrocyanides
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Pteridines
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Flavin-Adenine Dinucleotide
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6,7-dimethyl-8-ribityllumazine
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Deoxyribodipyrimidine Photo-Lyase