CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors

EMBO Rep. 2012 Mar 1;13(3):223-9. doi: 10.1038/embor.2012.2.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / classification
  • Bacterial Proteins / genetics
  • Binding Sites
  • Cryptochromes / chemistry*
  • Cryptochromes / classification
  • Cryptochromes / genetics
  • Crystallography, X-Ray
  • Deoxyribodipyrimidine Photo-Lyase / chemistry
  • Deoxyribodipyrimidine Photo-Lyase / genetics
  • Ferrocyanides / chemistry
  • Flavin-Adenine Dinucleotide / chemistry
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Phylogeny
  • Protein Binding
  • Protein Structure, Tertiary
  • Pteridines / chemistry
  • Rhodobacter sphaeroides / chemistry*
  • Rhodobacter sphaeroides / genetics
  • Sequence Alignment
  • Static Electricity

Substances

  • Bacterial Proteins
  • Cryptochromes
  • Ferrocyanides
  • Pteridines
  • Flavin-Adenine Dinucleotide
  • 6,7-dimethyl-8-ribityllumazine
  • Deoxyribodipyrimidine Photo-Lyase