Literature summary for 3.6.4.B7 extracted from

Lee, M.H.; Leng, C.H.; Chang, Y.C.; Chou, C.C.; Chen, Y.K.; Hsu, F.F.; Chang, C.S.; Wang, A.H., Wang, T.F.
Self-polymerization of archaeal RadA protein into long and fine helical filaments (2004), Biochem. Biophys. Res. Commun., 323, 845-851.

Search for more literature for 3.6.4.B7

Crystallization (Commentary)

Crystallization (Comment)	Organism
expression as a MBP-RadA-His6-fusion protein in Escherichia coli	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
large scale	Saccharolobus solfataricus

Subunits

Subunits	Comment	Organism
oligomer	Sso RadA proteins are capable of self-assembling into long and fine helical filaments up to 1 lm in length. This unusual protein filament exists not only in solution but also in RadA protein crystals without addition of any nucleotide cofactor. Sso RadA protein filament will dissemble upon incubation with ssDNA substrate and AMP-PNP, and then form only nucleoprotein filaments	Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
67	-	assay at	Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Saccharolobus solfataricus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)