2if9
Crystal Structure of SV40 T-antigen origin binding domain disulfide-linked dimer
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OverviewOverview
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.
About this StructureAbout this Structure
2IF9 is a Single protein structure of sequence from Simian virus 40. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the SV40 T-antigen origin binding domain in complex with DNA., Meinke G, Phelan P, Moine S, Bochkareva E, Bochkarev A, Bullock PA, Bohm A, PLoS Biol. 2007 Jan;5(2):e23. PMID:17253903
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