2Y32

Crystal structure of bradavidin

2Y32 の概要

• エントリーDOI: 10.2210/pdb2y32/pdb
• 分子名称: BLR5658 PROTEIN (2 entities in total)
• 機能のキーワード: biotin-binding protein
• 由来する生物種: BRADYRHIZOBIUM JAPONICUM
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57566.62

構造登録者

Leppiniemi, J.,Gronroos, T.,Johnson, M.S.,Kulomaa, M.S.,Hytonen, V.P.,Airenne, T.T. (登録日: 2010-12-17, 公開日: 2011-12-28, 最終更新日: 2024-10-16)

主引用文献

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

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: 22574129
DOI: 10.1371/JOURNAL.PONE.0035962

実験手法

X-RAY DIFFRACTION (1.78 Å)