1STP

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

1STP の概要

• エントリーDOI: 10.2210/pdb1stp/pdb
• 分子名称: STREPTAVIDIN COMPLEX WITH BIOTIN, BIOTIN (3 entities in total)
• 機能のキーワード: biotin binding protein
• 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: 1
• 化学式量合計: 16749.16

構造登録者

Weber, P.C.,Salemme, F.R. (登録日: 1992-03-12, 公開日: 1992-10-15, 最終更新日: 2024-02-14)

主引用文献

Weber, P.C.,Ohlendorf, D.H.,Wendoloski, J.J.,Salemme, F.R.
Structural origins of high-affinity biotin binding to streptavidin.
Science, 243:85-88, 1989

PubMed Abstract: The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.

PubMed: 2911722

実験手法

X-RAY DIFFRACTION (2.6 Å)