2itl: Difference between revisions

Revision as of 23:26, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2itl.png

Template:STRUCTURE 2itl

The origin binding domain of the SV40 large T antigen bound to the functional pen palindrome DNA (23 bp)The origin binding domain of the SV40 large T antigen bound to the functional pen palindrome DNA (23 bp)

Template:ABSTRACT PUBMED 17139255

About this StructureAbout this Structure

2ITL is a Single protein structure of sequence from Simian virus 40. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the origin-binding domain of simian virus 40 large T antigen bound to DNA., Bochkareva E, Martynowski D, Seitova A, Bochkarev A, EMBO J. 2006 Dec 13;25(24):5961-9. Epub 2006 Nov 30. PMID:17139255

Page seeded by OCA on Mon Jul 28 23:26:49 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The origin binding domain of the SV40 large T antigen bound to the functional pen palindrome DNA (23 bp)'''
+===The origin binding domain of the SV40 large T antigen bound to the functional pen palindrome DNA (23 bp)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17139255}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17139255 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17139255}}
 ==About this Structure==
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 [[Category: Seitova, A]]
 [[Category: Dna binding protein]]
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