The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins

Jenni Leppiniemi, Amit Meir, Niklas Kahkonen, Sampo Kukkurainen, Juha A. Maatta, Markus Ojanen, Janne Janis, Markku S. Kulomaa, Oded Livnah, Vesa P. Hytonen

Research output: Contribution to journalArticlepeer-review


Bradavidin II is a biotin-binding protein from Bradyrhizobium japonicum that resembles chicken avidin and bacterial streptavidin. A biophysical characterization was carried out using dynamic light scattering, native mass spectrometry, differential scanning calorimetry, and isothermal titration calorimetry combined with structural characterization using X-ray crystallography. These observations revealed that bradavidin II differs from canonical homotetrameric avidin protein family members in its quaternary structure. In contrast with the other avidins, bradavidin II appears to have a dynamic (transient) oligomeric state in solution. It is monomeric at low protein concentrations but forms higher oligomeric assemblies at higher concentrations. The crystal structure of bradavidin II revealed an important role for Phe42 in shielding the bound ligand from surrounding water molecules, thus functionally replacing the L7,8 loop essential for tight ligand binding in avidin and streptavidin. This bradavidin II characterization opens new avenues for oligomerizationindependent biotin-binding protein development.

Original languageAmerican English
Pages (from-to)980-994
Number of pages15
JournalProtein Science
Issue number7
StatePublished - Jul 2013


  • Dynamic structure
  • Ligand binding
  • Oligomeric state
  • Structural cooperativity

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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