2FUF

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

Summary for 2FUF

• Entry DOI: 10.2210/pdb2fuf/pdb
• Related: 1TBD
• Descriptor: Large T antigen, CITRATE ANION (3 entities in total)
• Functional Keywords: replication origin binding domain, dna replication, dna binding protein
• Biological source: Simian virus 40
• Cellular location: Host nucleus : P03070
• Total number of polymer chains: 1
• Total formula weight: 15697.52

Authors

Meinke, G.,Bullock, P.A.,Bohm, A. (deposition date: 2006-01-26, release date: 2006-08-22, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.45 Å)