2NTC

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

Summary for 2NTC

• Entry DOI: 10.2210/pdb2ntc/pdb
• Related: 1TBD 2FUF
• Descriptor: 21-nt PEN element of the SV40 DNA origin, large T antigen, ... (4 entities in total)
• Functional Keywords: origin binding domain; protein-dna complex; replication, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Simian virus 40
• Cellular location: Host nucleus: P03070
• Total number of polymer chains: 4
• Total formula weight: 43717.59

Authors

Bohm, A.,Meinke, G.,Bullock, P.A. (deposition date: 2006-11-07, release date: 2007-02-13, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)