3MG5

Core-streptavidin mutant F130L in complex with biotin

3MG5 の概要

• エントリーDOI: 10.2210/pdb3mg5/pdb
• 関連するPDBエントリー: 1MK5
• 分子名称: Streptavidin, BIOTIN, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: biotin-binding protein, streptavidin
• 由来する生物種: Streptomyces avidinii
• 細胞内の位置: Secreted: P22629
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 54979.55

構造登録者

Le Trong, I.,Baugh, L.,Stayton, P.S.,Lybrand, T.P.,Stenkamp, R.E. (登録日: 2010-04-05, 公開日: 2010-05-26, 最終更新日: 2023-09-06)

主引用文献

Baugh, L.,Le Trong, I.,Cerutti, D.S.,Gulich, S.,Stayton, P.S.,Stenkamp, R.E.,Lybrand, T.P.
A distal point mutation in the streptavidin-biotin complex preserves structure but diminishes binding affinity: experimental evidence of electronic polarization effects?
Biochemistry, 49:4568-4570, 2010

PubMed Abstract: We have identified a distal point mutation in streptavidin that causes a 1000-fold reduction in biotin binding affinity without disrupting the equilibrium complex structure. The F130L mutation creates a small cavity occupied by a water molecule; however, all neighboring side chain positions are preserved, and protein-biotin hydrogen bonds are unperturbed. Molecular dynamics simulations reveal a reduced mobility of biotin binding residues but no observable destabilization of protein-ligand interactions. Our combined structural and computational studies suggest that the additional water molecule may affect binding affinity through an electronic polarization effect that impacts the highly cooperative hydrogen bonding network in the biotin binding pocket.

PubMed: 20462252
DOI: 10.1021/bi1005392

実験手法

X-RAY DIFFRACTION (1.3 Å)