Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the single-stranded DNA-binding protein from Thermus aquaticus has been solved and refined at 1.85 A resolution. Two monomers, each encompassing two oligonucleotide/oligosaccharide-binding (OB) domains and a number of flexible beta-hairpin loops, form an oligomer of approximate D(2) symmetry typical of bacterial SSBs. Comparison with other SSB structures confirms considerable variability in the mode of oligomerization and aggregation of SSB oligomers.
Structure of the single-stranded DNA-binding protein SSB from Thermus aquaticus.,Jedrzejczak R, Dauter M, Dauter Z, Olszewski M, Dlugolecka A, Kur J Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1407-12. Epub 2006, Oct 18. PMID:17057346[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jedrzejczak R, Dauter M, Dauter Z, Olszewski M, Dlugolecka A, Kur J. Structure of the single-stranded DNA-binding protein SSB from Thermus aquaticus. Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1407-12. Epub 2006, Oct 18. PMID:17057346 doi:http://dx.doi.org/10.1107/S0907444906036031
