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4GGR

The structure of apo bradavidin2 (Form A)

Summary for 4GGR
Entry DOI10.2210/pdb4ggr/pdb
Related2Y32 4GGT 4GGZ
DescriptorBradavidin 2 (2 entities in total)
Functional Keywordsbradavidin, avidin, oligomeric state, streptavidin, high affinity systems, lipocalin fold, beta barrel, biotin binding protein
Biological sourceBradyrhizobium japonicum
Total number of polymer chains1
Total formula weight12581.16
Authors
Livnah, O.,Meir, A. (deposition date: 2012-08-07, release date: 2013-06-19, Last modification date: 2024-10-09)
Primary citationLeppiniemi, J.,Meir, A.,Kahkonen, N.,Kukkurainen, S.,Maatta, J.A.,Ojanen, M.,Janis, J.,Kulomaa, M.S.,Livnah, O.,Hytonen, V.P.
The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins.
Protein Sci., 22:980-994, 2013
Cited by
PubMed 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.
PubMed: 23661323
DOI: 10.1002/pro.2281
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

226707

數據於2024-10-30公開中

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