ArticleProtein science : a publication of the Protein Society2013
The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- An Analysis of the Biotin-(Strept)avidin System in Immunoassays: Interference and Mitigation Strategies.Current issues in molecular biology · 2023Review
- Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Bacterial avidins are a widely distributed protein family in Actinobacteria, Proteobacteria and Bacteroidetes.BMC ecology and evolution · 2021Article
- Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity.Scientific reports · 2020Article
- Functional expression of monomeric streptavidin and fusion proteins in Escherichia coli: applications in flow cytometry and ELISA.Applied microbiology and biotechnology · 2018Article
- Article
- Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi.Veterinary microbiology · 2015Article
- Structure of the virulence-associated protein VapD from the intracellular pathogen Rhodococcus equi.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Article
- Zebavidin--an avidin-like protein from zebrafish.PloS one · 2013Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 oligomerization-independent biotin-binding protein development.
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