2fuf: Difference between revisions

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New page: left|200px<br /><applet load="2fuf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fuf, resolution 1.450Å" /> '''Crystal structure o...
 
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[[Image:2fuf.gif|left|200px]]<br /><applet load="2fuf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2fuf.gif|left|200px]]<br /><applet load="2fuf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2fuf, resolution 1.450&Aring;" />
caption="2fuf, resolution 1.450&Aring;" />
'''Crystal structure of the SV40 large T antigen origin-binding domain'''<br />
'''Crystal structure of the SV40 large T antigen origin-binding domain'''<br />


==Overview==
==Overview==
The origins of replication of DNA tumor viruses have a highly conserved, feature, namely, multiple binding sites for their respective initiator, proteins arranged as inverted repeats. In the 1.45-angstroms crystal, structure of the simian virus 40 large T-antigen (T-ag) origin-binding, domain (obd) reported herein, T-ag obd monomers form a left-handed spiral, with an inner channel of 30 angstroms having six monomers per turn. The, inner surface of the spiral is positively charged and includes residues, known to bind DNA. Residues implicated in hexamerization of full-length, T-ag are located at the interface between adjacent T-ag obd monomers., These data provide a high-resolution model of the hexamer of, origin-binding domains observed in electron microscopy studies and allow, the obd's to be oriented relative to the hexamer of T-ag helicase domains, to which they are connected.
The origins of replication of DNA tumor viruses have a highly conserved feature, namely, multiple binding sites for their respective initiator proteins arranged as inverted repeats. In the 1.45-angstroms crystal structure of the simian virus 40 large T-antigen (T-ag) origin-binding domain (obd) reported herein, T-ag obd monomers form a left-handed spiral with an inner channel of 30 angstroms having six monomers per turn. The inner surface of the spiral is positively charged and includes residues known to bind DNA. Residues implicated in hexamerization of full-length T-ag are located at the interface between adjacent T-ag obd monomers. These data provide a high-resolution model of the hexamer of origin-binding domains observed in electron microscopy studies and allow the obd's to be oriented relative to the hexamer of T-ag helicase domains to which they are connected.


==About this Structure==
==About this Structure==
2FUF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40] with FLC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FUF OCA].  
2FUF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40] with <scene name='pdbligand=FLC:'>FLC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUF OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bohm, A.]]
[[Category: Bohm, A.]]
[[Category: Bullock, P.A.]]
[[Category: Bullock, P A.]]
[[Category: Meinke, G.]]
[[Category: Meinke, G.]]
[[Category: FLC]]
[[Category: FLC]]
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[[Category: replication origin binding domain]]
[[Category: replication origin binding domain]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:46:41 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:15 2008''

Revision as of 18:25, 21 February 2008

File:2fuf.gif


2fuf, resolution 1.450Å

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Crystal structure of the SV40 large T antigen origin-binding domain

OverviewOverview

The origins of replication of DNA tumor viruses have a highly conserved feature, namely, multiple binding sites for their respective initiator proteins arranged as inverted repeats. In the 1.45-angstroms crystal structure of the simian virus 40 large T-antigen (T-ag) origin-binding domain (obd) reported herein, T-ag obd monomers form a left-handed spiral with an inner channel of 30 angstroms having six monomers per turn. The inner surface of the spiral is positively charged and includes residues known to bind DNA. Residues implicated in hexamerization of full-length T-ag are located at the interface between adjacent T-ag obd monomers. These data provide a high-resolution model of the hexamer of origin-binding domains observed in electron microscopy studies and allow the obd's to be oriented relative to the hexamer of T-ag helicase domains to which they are connected.

About this StructureAbout this Structure

2FUF is a Single protein structure of sequence from Simian virus 40 with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the simian virus 40 large T-antigen origin-binding domain., Meinke G, Bullock PA, Bohm A, J Virol. 2006 May;80(9):4304-12. PMID:16611889

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