Structural characterization of core-bradavidin in complex with biotin

@article{Agrawal2017StructuralCO,
  title={Structural characterization of core-bradavidin in complex with biotin},
  author={N. Agrawal and J. M{\"a}{\"a}tt{\"a} and M. Kulomaa and V. Hyt{\"o}nen and M. S. Johnson and T. Airenne},
  journal={PLoS ONE},
  year={2017},
  volume={12}
}
Bradavidin is a tetrameric biotin-binding protein similar to chicken avidin and bacterial streptavidin, and was originally cloned from the nitrogen-fixing bacteria Bradyrhizobium diazoefficiens. We have previously reported the crystal structure of the full-length, wild-type (wt) bradavidin with 138 amino acids, where the C-terminal residues Gly129-Lys138 (“Brad-tag”) act as an intrinsic ligand (i.e. Gly129-Lys138 bind into the biotin-binding site of an adjacent subunit within the same tetramer… Expand
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References

SHOWING 1-10 OF 84 REFERENCES
Structure of Bradavidin – C-Terminal Residues Act as Intrinsic Ligands
  • 11
  • PDF
Bradavidin II from Bradyrhizobium japonicum: a new avidin-like biotin-binding protein.
  • 33
The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins
  • 17
Three-dimensional structures of avidin and the avidin-biotin complex.
  • 497
  • PDF
Rational Design of an Active Avidin Monomer*
  • 80
Hoefavidin: A dimeric bacterial avidin with a C-terminal binding tail.
  • 16
  • Highly Influential
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