2ntc

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(New page: 200px<br /><applet load="2ntc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ntc, resolution 2.40&Aring;" /> '''Crystal Structure of...)
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==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17253903 17253903]
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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 Feb;5(2):e23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17253903 17253903]
[[Category: Simian virus 40]]
[[Category: Simian virus 40]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bohm, A.]]
[[Category: Bohm, A.]]
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[[Category: Bullock, P.A.]]
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[[Category: Bullock, P A.]]
[[Category: Meinke, G.]]
[[Category: Meinke, G.]]
[[Category: origin binding domain; protein-dna complex; replication]]
[[Category: origin binding domain; protein-dna complex; replication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:59:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:45 2008''

Revision as of 16:10, 21 February 2008


2ntc, resolution 2.40Å

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

Overview

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 Structure

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

Reference

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 Feb;5(2):e23. PMID:17253903

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