2NTC

Crystal Structure of sv40 large T antigen origin binding domain with DNA

2NTC の概要

• エントリーDOI: 10.2210/pdb2ntc/pdb
• 関連するPDBエントリー: 1TBD 2FUF
• 分子名称: 21-nt PEN element of the SV40 DNA origin, large T antigen, ... (4 entities in total)
• 機能のキーワード: origin binding domain; protein-dna complex; replication, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Simian virus 40
• 細胞内の位置: Host nucleus: P03070
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 43717.59

構造登録者

Bohm, A.,Meinke, G.,Bullock, P.A. (登録日: 2006-11-07, 公開日: 2007-02-13, 最終更新日: 2024-04-03)

主引用文献

Meinke, G.,Phelan, P.,Moine, S.,Bochkareva, E.,Bochkarev, A.,Bullock, P.A.,Bohm, A.
The Crystal Structure of the SV40 T-Antigen Origin Binding Domain in Complex with DNA
Plos Biol., 5:e23-e23, 2007

PubMed Abstract: DNA replication is initiated upon binding of "initiators" to origins of replication. In simian virus 40 (SV40), the core origin contains four pentanucleotide binding sites organized as pairs of inverted repeats. Here we describe the crystal structures of the origin binding domain (obd) of the SV40 large T-antigen (T-ag) both with and without a subfragment of origin-containing DNA. In the co-structure, two T-ag obds are oriented in a head-to-head fashion on the same face of the DNA, and each T-ag obd engages the major groove. Although the obds are very close to each other when bound to this DNA target, they do not contact one another. These data provide a high-resolution structural model that explains site-specific binding to the origin and suggests how these interactions help direct the oligomerization events that culminate in assembly of the helicase-active dodecameric complex of T-ag.

PubMed: 17253903
DOI: 10.1371/journal.pbio.0050023

実験手法

X-RAY DIFFRACTION (2.4 Å)