4FGN

Crystal structure of the SV40 large T-antigen origin bining domain bound to Site I DNA

4FGN の概要

• エントリーDOI: 10.2210/pdb4fgn/pdb
• 関連するPDBエントリー: 2FUF 2ITL 2NTC
• 分子名称: Large T antigen, Site I DNA, ... (4 entities in total)
• 機能のキーワード: origin binding domain, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Simian virus 40 (SV40); 詳細
• 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: 44603.08

構造登録者

Meinke, G.,Bohm, A.,Bullock, P.A. (登録日: 2012-06-04, 公開日: 2013-01-23, 最終更新日: 2023-09-13)

主引用文献

Meinke, G.,Phelan, P.J.,Harrison, C.J.,Bullock, P.A.
Analysis of the Costructure of the Simian Virus 40 T-Antigen Origin Binding Domain with Site I Reveals a Correlation between GAGGC Spacing and Spiral Assembly.
J.Virol., 87:2923-2934, 2013

PubMed Abstract: Polyomavirus origins of replication contain multiple occurrences of G(A/G)GGC, the high-affinity binding element for the viral initiator T-antigen (T-ag). The site I regulatory region of simian virus 40, involved in the repression of transcription and the enhancement of DNA replication initiation, contains two GAGGC sequences arranged head to tail and separated by a 7-bp AT-rich sequence. We have solved a 3.2-Å costructure of the SV40 origin-binding domain (OBD) bound to site I. We have also established that T-ag assembly on site I is limited to the formation of a single hexamer. These observations have enabled an analysis of the role(s) of the OBDs bound to the site I pentanucleotides in hexamer formation. Of interest, they reveal a correlation between the OBDs bound to site I and a pair of OBD subunits in the previously described hexameric spiral structure. Based on these findings, we propose that spiral assembly is promoted by pentanucleotide pairs arranged in a head-to-tail manner. Finally, the possibility that spiral assembly by OBD subunits accounts for the heterogeneous distribution of pentanucleotides found in the origins of replication of polyomaviruses is discussed.

PubMed: 23269808
DOI: 10.1128/JVI.02549-12

実験手法

X-RAY DIFFRACTION (3.2 Å)