2ipr: Difference between revisions

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[[Image:2ipr.gif|left|200px]]
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{{STRUCTURE_2ipr|  PDB=2ipr  |  SCENE=  }}  
{{STRUCTURE_2ipr|  PDB=2ipr  |  SCENE=  }}  


'''Origin binding domain of the SV40 large T antigen (residues 131-259). P21 crystal form'''
===Origin binding domain of the SV40 large T antigen (residues 131-259). P21 crystal form===




==Overview==
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The large T antigen (T-ag) protein binds to and activates DNA replication from the origin of DNA replication (ori) in simian virus 40 (SV40). Here, we determined the crystal structures of the T-ag origin-binding domain (OBD) in apo form, and bound to either a 17 bp palindrome (sites 1 and 3) or a 23 bp ori DNA palindrome comprising all four GAGGC binding sites for OBD. The T-ag OBDs were shown to interact with the DNA through a loop comprising Ser147-Thr155 (A1 loop), a combination of a DNA-binding helix and loop (His203-Asn210), and Asn227. The A1 loop traveled back-and-forth along the major groove and accounted for most of the sequence-determining contacts with the DNA. Unexpectedly, in both T-ag-DNA structures, the T-ag OBDs bound DNA independently and did not make direct protein-protein contacts. The T-ag OBD was also captured bound to a non-consensus site ATGGC even in the presence of its canonical site GAGGC. Our observations taken together with the known biochemical and structural features of the T-ag-origin interaction suggest a model for origin unwinding.
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{{ABSTRACT_PUBMED_17139255}}


==About this Structure==
==About this Structure==
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[[Category: Martynowski, D.]]
[[Category: Martynowski, D.]]
[[Category: Dna binding protein]]
[[Category: Dna binding protein]]
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