Biology:DNA photolyase N-terminal domain
| DNA photolyase, N-terminal | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | DNA_photolyase | ||||||||
| Pfam | PF00875 | ||||||||
| InterPro | IPR006050 | ||||||||
| PROSITE | PDOC00331 | ||||||||
| SCOP2 | 1qnf / SCOPe / SUPFAM | ||||||||
| |||||||||
| FeS-BCP | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | DPRP | ||||||||
| Pfam | PF04244 | ||||||||
| InterPro | IPR007357 | ||||||||
| |||||||||
DNA photolyase, N-terminal is an evolutionary conserved protein domain. This domain binds a light harvesting chromophore that enhanced the spectrum of photolyase or cryptochrome light absorption, i.e. an antenna.[1] It adopts the rossmann fold.[2]
The cofactor may be either the pterin 5,10-Methenyltetrahydrofolate (MTHF, MHF) in folate photolyases (PDB: 4U63) or the deazaflavin 8-hydroxy-7,8-didemethyl-5-deazariboflavin (8-HDF, FO1) in deazaflavin photolyases (PDB: 3CVV, 4CDN).[2] The 8-HDF ligand usually binds into this domain (next to the C-terminal half), while MHF tends to bind to an outside groove of this domain.[3] A structural signature for 8-HDF binding has been produced, highlighting amino acid residues that determine which antenna a photolyase can use.[4] Experiments on a Thermus thermophilus protein with this domain (P61497) shows that artificial substrates can be alternatively used for a modified absorption spectra. It naturally binds FMN in a pose similar to 8-HDF.[5] In addition, many cryptochromes, especially those from animals, bind no cofactors at this domain.[3]
Even though few eukaryotes (and no animals) can synthesize 8-HDF on their own,[6] many lineages nevertheless use deazaflavin photolyases. They probably receive 8-HDF from their endosymbiotic microbes.[4] Unlike many bacterial deazaflavin photolyases that accepts FMN as well as 8-HDF, one such enzyme from the fruit fly only accepts 8-HDF.[6]
The FeS-BCP N-terminal domain is homologous to this domain. Instead of an organic cofactor, its chromophore is an iron-sulphur cluster.[7]
Examples
Human proteins containing this domain include:
- CRY1
- CRY2
References
- ↑ "Crystal structure of DNA photolyase from Anacystis nidulans". Nature Structural Biology 4 (11): 887–91. November 1997. doi:10.1038/nsb1197-887. PMID 9360600.
- ↑ 2.0 2.1 "Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors". Chemical Reviews 103 (6): 2203–37. June 2003. doi:10.1021/cr0204348. PMID 12797829.
- ↑ 3.0 3.1 "The class III cyclobutane pyrimidine dimer photolyase structure reveals a new antenna chromophore binding site and alternative photoreduction pathways". The Journal of Biological Chemistry 290 (18): 11504–14. May 2015. doi:10.1074/jbc.M115.637868. PMID 25784552.
- ↑ 4.0 4.1 "Structural and evolutionary aspects of antenna chromophore usage by class II photolyases". The Journal of Biological Chemistry 289 (28): 19659–69. July 2014. doi:10.1074/jbc.M113.542431. PMID 24849603.
- ↑ "Natural and non-natural antenna chromophores in the DNA photolyase from Thermus thermophilus". ChemBioChem 7 (11): 1798–806. November 2006. doi:10.1002/cbic.200600206. PMID 17051659.
- ↑ 6.0 6.1 "The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes". Proceedings of the National Academy of Sciences of the United States of America 106 (28): 11540–5. July 2009. doi:10.1073/pnas.0812665106. PMID 19570997.
- ↑ "A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster". PLOS ONE 6 (10): e26775. 31 October 2011. doi:10.1371/journal.pone.0026775. PMID 22066008. Bibcode: 2011PLoSO...626775O.
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