2y32

Crystal structure of bradavidinCrystal structure of bradavidin

Structural highlights 2y32 is a 4 chain structure with sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q89IH6_BRADU Publication Abstract from PubMed 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 approximately 25 microM 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. Structure of bradavidin - C-terminal residues act as intrinsic ligands.,Leppiniemi J, Gronroos T, Maatta JA, Johnson MS, Kulomaa MS, Hytonen VP, Airenne TT PLoS One. 2012;7(5):e35962. Epub 2012 May 4. PMID:22574129 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2y32, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image