Literature summary for 4.1.99.3 extracted from

Fujihashi, M.; Numoto, N.; Kobayashi, Y.; Mizushima, A.; Tsujimura, M.; Nakamura, A.; Kawarabayasi, Y.; Miki, K.
Crystal structure of archaeal photolyase from Sulfolobus tokodaii with two FAD molecules: implication of a novel light-harvesting cofactor (2007), J. Mol. Biol., 365, 903-910.

Cloned(Commentary)

Cloned (Comment)	Organism
cloned in Escherichia coli as a C-terminal His-tagged fusion protein	Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the protein is determined at 2.8 A resolution with the molecular replacement method. Crystal structure of the St-photolyase is superimposed very well on the three known photolyases from Escherichia coli, Anacystis nidulans and Thermus thermophilus including the catalytic cofactor FAD. Surprisingly, another FAD molecule is found at the position of the light-harvesting cofactor. This second FAD molecule is well accommodated in the crystal structure, suggesting that FAD works as a novel light-harvesting cofactor of photolyase. In addition, two of the four CPD recognition residues in the crystal structure of Anacystis nidulans are not found in St-photolyase, indicating that St-photolyase might recognize cyclobutane pyrimidine dimer with a geometry different from that of Anphotolyase. RCSB PDB accession code: 2E0I	Sulfurisphaera tokodaii

Crystallization (Comment)

Organism

crystal structure of the protein is determined at 2.8 A resolution with the molecular replacement method. Crystal structure of the St-photolyase is superimposed very well on the three known photolyases from Escherichia coli, Anacystis nidulans and Thermus thermophilus including the catalytic cofactor FAD. Surprisingly, another FAD molecule is found at the position of the light-harvesting cofactor. This second FAD molecule is well accommodated in the crystal structure, suggesting that FAD works as a novel light-harvesting cofactor of photolyase. In addition, two of the four CPD recognition residues in the crystal structure of Anacystis nidulans are not found in St-photolyase, indicating that St-photolyase might recognize cyclobutane pyrimidine dimer with a geometry different from that of Anphotolyase. RCSB PDB accession code: 2E0I

Sulfurisphaera tokodaii

Organism

Organism	UniProt	Comment	Textmining
Sulfurisphaera tokodaii	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
protein is purified using Ni-NTA and hydrophobic columns	Sulfurisphaera tokodaii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	protein shows phoreactive activity determined by UV/Vis-spectroscopy at 265 nm	Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
cyclobutadipyrimidine in DNA	-	Sulfurisphaera tokodaii	2 pyrimidine residues in DNA	-	?

Synonyms

Synonyms	Comment	Organism
photolyase	-	Sulfurisphaera tokodaii
St-photolyase	-	Sulfurisphaera tokodaii

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Sulfurisphaera tokodaii