3RY2

Wild-type core streptavidin-biotin complex at atomic resolution

3RY2 の概要

• エントリーDOI: 10.2210/pdb3ry2/pdb
• 関連するPDBエントリー: 3RY1
• 分子名称: Streptavidin, BIOTIN, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: biotin-binding protein, biotin
• 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: 2
• 化学式量合計: 27327.58

構造登録者

Stenkamp, R.E.,Le Trong, I.,Stayton, P.S.,Lybrand, T.P. (登録日: 2011-05-10, 公開日: 2011-08-24, 最終更新日: 2023-09-13)

主引用文献

Le Trong, I.,Wang, Z.,Hyre, D.E.,Lybrand, T.P.,Stayton, P.S.,Stenkamp, R.E.
Streptavidin and its biotin complex at atomic resolution.
Acta Crystallogr.,Sect.D, 67:813-821, 2011

PubMed Abstract: Atomic resolution crystallographic studies of streptavidin and its biotin complex have been carried out at 1.03 and 0.95 Å, respectively. The wild-type protein crystallized with a tetramer in the asymmetric unit, while the crystals of the biotin complex contained two subunits in the asymmetric unit. Comparison of the six subunits shows the various ways in which the protein accommodates ligand binding and different crystal-packing environments. Conformational variation is found in each of the polypeptide loops connecting the eight strands in the β-sandwich subunit, but the largest differences are found in the flexible binding loop (residues 45-52). In three of the unliganded subunits the loop is in an `open' conformation, while in the two subunits binding biotin, as well as in one of the unliganded subunits, this loop `closes' over the biotin-binding site. The `closed' loop contributes to the protein's high affinity for biotin. Analysis of the anisotropic displacement parameters included in the crystallographic models is consistent with the variation found in the loop structures and the view that the dynamic nature of the protein structure contributes to the ability of the protein to bind biotin so tightly.

PubMed: 21904034
DOI: 10.1107/S0907444911027806

実験手法

X-RAY DIFFRACTION (0.95 Å)