1svl
From Proteopedia
(New page: 200px<br /><applet load="1svl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1svl, resolution 1.95Å" /> '''Co-crystal structure...) |
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| - | [[Image:1svl.gif|left|200px]]<br /><applet load="1svl" size=" | + | [[Image:1svl.gif|left|200px]]<br /><applet load="1svl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1svl, resolution 1.95Å" /> | caption="1svl, resolution 1.95Å" /> | ||
'''Co-crystal structure of SV40 large T antigen helicase domain and ADP'''<br /> | '''Co-crystal structure of SV40 large T antigen helicase domain and ADP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The large tumor antigen (LTag) of simian virus 40, an AAA(+) protein, is a | + | The large tumor antigen (LTag) of simian virus 40, an AAA(+) protein, is a hexameric helicase essential for viral DNA replication in eukaryotic cells. LTag functions as an efficient molecular machine powered by ATP binding and hydrolysis for origin DNA melting and replication fork unwinding. To understand how ATP binding and hydrolysis are coupled to conformational changes, we have determined high-resolution structures ( approximately 1.9 A) of LTag hexamers in distinct nucleotide binding states. The structural differences of LTag in various nucleotide states detail the molecular mechanisms of conformational changes triggered by ATP binding/hydrolysis and reveal a potential mechanism of concerted nucleotide binding and hydrolysis. During these conformational changes, the angles and orientations between domains of a monomer alter, creating an "iris"-like motion in the hexamer. Additionally, six unique beta hairpins on the channel surface move longitudinally along the central channel, possibly serving as a motor for pulling DNA into the LTag double hexamer for unwinding. |
==About this Structure== | ==About this Structure== | ||
| - | 1SVL 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 ZN, MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SVL 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=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Simian virus 40]] | [[Category: Simian virus 40]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chen, X | + | [[Category: Chen, X S.]] |
| - | [[Category: Finkielstein, C | + | [[Category: Finkielstein, C V.]] |
[[Category: Gai, D.]] | [[Category: Gai, D.]] | ||
[[Category: Zhao, R.]] | [[Category: Zhao, R.]] | ||
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[[Category: aaa+ fold]] | [[Category: aaa+ fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:42 2008'' |
Revision as of 13:05, 21 February 2008
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Co-crystal structure of SV40 large T antigen helicase domain and ADP
Overview
The large tumor antigen (LTag) of simian virus 40, an AAA(+) protein, is a hexameric helicase essential for viral DNA replication in eukaryotic cells. LTag functions as an efficient molecular machine powered by ATP binding and hydrolysis for origin DNA melting and replication fork unwinding. To understand how ATP binding and hydrolysis are coupled to conformational changes, we have determined high-resolution structures ( approximately 1.9 A) of LTag hexamers in distinct nucleotide binding states. The structural differences of LTag in various nucleotide states detail the molecular mechanisms of conformational changes triggered by ATP binding/hydrolysis and reveal a potential mechanism of concerted nucleotide binding and hydrolysis. During these conformational changes, the angles and orientations between domains of a monomer alter, creating an "iris"-like motion in the hexamer. Additionally, six unique beta hairpins on the channel surface move longitudinally along the central channel, possibly serving as a motor for pulling DNA into the LTag double hexamer for unwinding.
About this Structure
1SVL is a Single protein structure of sequence from Simian virus 40 with , and as ligands. Full crystallographic information is available from OCA.
Reference
Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen., Gai D, Zhao R, Li D, Finkielstein CV, Chen XS, Cell. 2004 Oct 1;119(1):47-60. PMID:15454080
Page seeded by OCA on Thu Feb 21 15:05:42 2008
Categories: Simian virus 40 | Single protein | Chen, X S. | Finkielstein, C V. | Gai, D. | Zhao, R. | ADP | MG | ZN | Aaa+ fold
