Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding.
@article{Bonin2004CrystalSO, title={Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding.}, author={I. Bonin and Rudolf Robelek and H. Benecke and H. Urlaub and A. Bacher and G. Richter and M. Wahl}, journal={The Biochemical journal}, year={2004}, volume={383 Pt. 3}, pages={ 419-28 } }
NusB is a prokaryotic transcription factor involved in antitermination processes, during which it interacts with the boxA portion of the mRNA nut site. Previous studies have shown that NusB exhibits an all-helical fold, and that the protein from Escherichia coli forms monomers, while Mycobacterium tuberculosis NusB is a dimer. The functional significance of NusB dimerization is unknown. We have determined five crystal structures of NusB from Thermotoga maritima. In three crystal forms the… CONTINUE READING
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