2Y32
Crystal structure of bradavidin
Summary for 2Y32
| Entry DOI | 10.2210/pdb2y32/pdb |
| Descriptor | BLR5658 PROTEIN (2 entities in total) |
| Functional Keywords | biotin-binding protein |
| Biological source | BRADYRHIZOBIUM JAPONICUM |
| Total number of polymer chains | 4 |
| Total formula weight | 57566.62 |
| Authors | Leppiniemi, J.,Gronroos, T.,Johnson, M.S.,Kulomaa, M.S.,Hytonen, V.P.,Airenne, T.T. (deposition date: 2010-12-17, release date: 2011-12-28, Last modification date: 2024-10-16) |
| Primary citation | Leppiniemi, J.,Gronroos, T.,Maatta, J.A.E.,Johnson, M.S.,Kulomaa, M.S.,Hytonen, V.P.,Airenne, T.T. Structure of Bradavidin - C-Terminal Residues Act as Intrinsic Ligands. Plos One, 7:35962-, 2012 Cited by PubMed Abstract: Bradavidin is a homotetrameric biotin-binding protein from Bradyrhizobium japonicum, a nitrogen fixing and root nodule-forming symbiotic bacterium of the soybean. Wild-type (wt) bradavidin has 138 amino acid residues, whereas the C-terminally truncated core-bradavidin has only 118 residues. We have solved the X-ray structure of wt bradavidin and found that the C-terminal amino acids of each subunit were uniquely bound to the biotin-binding pocket of an adjacent subunit. The biotin-binding pocket occupying peptide (SEKLSNTK) was named "Brad-tag" and it serves as an intrinsic stabilizing ligand in wt bradavidin. The binding of Brad-tag to core-bradavidin was analysed by isothermal titration calorimetry and a binding affinity of ∼25 µM was measured. In order to study the potential of Brad-tag, a green fluorescent protein tagged with Brad-tag was prepared and successfully concentrated from a bacterial cell lysate using core-bradavidin-functionalized Sepharose resin. PubMed: 22574129DOI: 10.1371/JOURNAL.PONE.0035962 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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