2FUF

Crystal structure of the SV40 large T antigen origin-binding domain

2FUF の概要

• エントリーDOI: 10.2210/pdb2fuf/pdb
• 関連するPDBエントリー: 1TBD
• 分子名称: Large T antigen, CITRATE ANION (3 entities in total)
• 機能のキーワード: replication origin binding domain, dna replication, dna binding protein
• 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: 1
• 化学式量合計: 15697.52

構造登録者

Meinke, G.,Bullock, P.A.,Bohm, A. (登録日: 2006-01-26, 公開日: 2006-08-22, 最終更新日: 2024-10-09)

主引用文献

Meinke, G.,Bullock, P.A.,Bohm, A.
Crystal structure of the simian virus 40 large T-antigen origin-binding domain.
J.Virol., 80:4304-4312, 2006

PubMed Abstract: The origins of replication of DNA tumor viruses have a highly conserved feature, namely, multiple binding sites for their respective initiator proteins arranged as inverted repeats. In the 1.45-angstroms crystal structure of the simian virus 40 large T-antigen (T-ag) origin-binding domain (obd) reported herein, T-ag obd monomers form a left-handed spiral with an inner channel of 30 angstroms having six monomers per turn. The inner surface of the spiral is positively charged and includes residues known to bind DNA. Residues implicated in hexamerization of full-length T-ag are located at the interface between adjacent T-ag obd monomers. These data provide a high-resolution model of the hexamer of origin-binding domains observed in electron microscopy studies and allow the obd's to be oriented relative to the hexamer of T-ag helicase domains to which they are connected.

PubMed: 16611889
DOI: 10.1128/JVI.80.9.4304-4312.2006

実験手法

X-RAY DIFFRACTION (1.45 Å)