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Literature summary for 4.1.99.3 extracted from
- Structural biology of DNA photolyases and cryptochromes (2009), Curr. Opin. Struct. Biol., 19, 277-285.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| photolyase-like domain of Cry1 | Arabidopsis thaliana |
| shows an N-terminal alpha/beta domain and a C-terminal alpha-helical domain | Escherichia coli |
| shows an N-terminal alpha/beta domain and a C-terminal alpha-helical domain. In complex with a DNA-duplex containing a synthetic cyclobutane-pyrimidine-dimers lesion analog, which shows that the protein fold changes only marginally upon DNA binding. CPD-photolyase proteins fully open the DNA-duplex structure at the damaged site and flip the dinucleotide lesion out of the duplex into the active site. Lesion comes in close contact (3 A) with the active FADH-cofactor | Synechococcus elongatus PCC 7942 = FACHB-805 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Escherichia coli | P00914 | - |
- |
| Homo sapiens | - |
- |
- |
| Sulfurisphaera tokodaii | - |
- |
- |
| Synechococcus elongatus PCC 7942 = FACHB-805 | - |
- |
- |
| Thermus thermophilus | P61497 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| adenosine 5'-(beta,gamma-imido)triphosphate | Cry1 | Arabidopsis thaliana | ? | - |
? |  |
| additional information | CPD-photolyase is a DNA repair protein, the electron-transport chain of Cry1 involves a Tyr residue as initial electron donor. For Cry3, weak but unspecific DNA binding, for Cry1, DNA binding cannot be detected. Cry2, whose surface largely resembles that of Cry1, does bind to DNA. Cry3 does repair cyclobutane-pyrimidine-dimers when the lesion is located in a preflipped out state such as in bulges of dsDNA. DASH cryptochromes are single-strand-specific CPD-photolyases | Arabidopsis thaliana | ? | - |
? | |
| additional information | Cry2 protein binds to ssDNA with high affinity | Homo sapiens | ? | - |
? | |
| additional information | DNA repair protein | Synechococcus elongatus PCC 7942 = FACHB-805 | ? | - |
? | |
| additional information | DNA repair protein | Escherichia coli | ? | - |
? | |
| thymine | - |
Thermus thermophilus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CPD-photolyase | - |
Synechococcus elongatus PCC 7942 = FACHB-805 |
| CPD-photolyase | - |
Homo sapiens |
| CPD-photolyase | - |
Arabidopsis thaliana |
| CPD-photolyase | - |
Sulfurisphaera tokodaii |
| CPD-photolyase | - |
Thermus thermophilus |
| CPD-photolyase | - |
Escherichia coli |
| CPD-Phr | - |
Sulfurisphaera tokodaii |
| CPD-Phr | - |
Thermus thermophilus |
| CPD-Phr | - |
Escherichia coli |
| Cry-DASH | - |
Arabidopsis thaliana |
| Cry1 | - |
Homo sapiens |
| Cry1 | - |
Arabidopsis thaliana |
| Cry2 | - |
Homo sapiens |
| Cry2 | - |
Arabidopsis thaliana |
| cry3 | - |
Arabidopsis thaliana |
| cryptochrome-DASH | - |
Arabidopsis thaliana |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 5,10-methenyltetrahydrofolate | bound at the interface between N-terminal and C-terminal domain | Synechococcus elongatus PCC 7942 = FACHB-805 | |
| 5,10-methenyltetrahydrofolate | bound at the interface between N-terminal and C-terminal domain | Escherichia coli | |
| 5,10-methenyltetrahydrofolate | Cry3 | Arabidopsis thaliana | |
| 8-hydroxy-5-deazariboflavin | bound at the interface between N-terminal and C-terminal domain | Synechococcus elongatus PCC 7942 = FACHB-805 | |
| 8-hydroxy-5-deazariboflavin | bound at the interface between N-terminal and C-terminal domain | Escherichia coli | |
| 8-hydroxy-5-deazariboflavin | photolyase can bind next to the natural cofactor 8-hydroxy-5-deazariboflavin also FMN | Thermus thermophilus | |
| 8-iodo-8-demethylriboflavin | - |
Thermus thermophilus | |
| FAD | a second FAD molecule is present in the antenna pigment binding pocket | Sulfurisphaera tokodaii | |
| FAD | alpha-helical domain is harboring the FAD cofactor, essential for catalysis | Synechococcus elongatus PCC 7942 = FACHB-805 | |
| FAD | alpha-helical domain is harboring the FAD cofactor, essential for catalysis | Escherichia coli | |
| FAD | Cry1, which does not bind to DNA, possesses a strongly reduced surface charge around the FAD binding pocket | Arabidopsis thaliana | |
| FADH2 | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | |
| FMN | photolyase can bind next to the natural cofactor 8-hydroxy-5-deazariboflavin also FMN | Thermus thermophilus | |
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