2P0J

Structure of restriction endonuclease BstYI bound to non-cognate DNA

2P0J の概要

• エントリーDOI: 10.2210/pdb2p0j/pdb
• 関連するPDBエントリー: 1SD0 1VRR
• 分子名称: 5'-D(*AP*TP*GP*AP*AP*TP*CP*CP*AP*TP*A)-3', 5'-D(*TP*AP*TP*GP*GP*AP*TP*TP*CP*AP*T)-3', BstYI, ... (4 entities in total)
• 機能のキーワード: restriction endonuclease, dna recognition, scanning, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 53149.79

構造登録者

Townson, S.A.,Samuelson, J.C.,Bao, Y.,Xu, S.Y.,Aggarwal, A.K. (登録日: 2007-02-28, 公開日: 2007-05-01, 最終更新日: 2024-02-21)

主引用文献

Townson, S.A.,Samuelson, J.C.,Bao, Y.,Xu, S.Y.,Aggarwal, A.K.
BstYI Bound to Noncognate DNA Reveals a "Hemispecific" Complex: Implications for DNA Scanning.
Structure, 15:449-459, 2007

PubMed Abstract: DNA recognition by proteins is essential for specific expression of genes in a living organism. En route to a target DNA site, a protein will often sample noncognate DNA sites through nonspecific protein-DNA interactions, resulting in a variety of conformationally different binding states. We present here the crystal structure of endonuclease BstYI bound to a noncognate DNA. Surprisingly, the structure reveals the enzyme in a "hemispecific" binding state on the pathway between nonspecific and specific recognition. A single base pair change in the DNA abolishes binding of only one monomer, with the second monomer bound specifically. We show that the enzyme binds essentially as a rigid body, and that one end of the DNA is accommodated loosely in the binding cleft while the other end is held tightly. Another intriguing feature of the structure is Ser172, which has a dual role in establishing nonspecific and specific contacts. Taken together, the structure provides a snapshot of an enzyme in a "paused" intermediate state that may be part of a more general mechanism of scanning DNA.

PubMed: 17437717
DOI: 10.1016/j.str.2007.03.002

実験手法

X-RAY DIFFRACTION (2.1 Å)