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1svl

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[[Image:1svl.gif|left|200px]]
[[Image:1svl.gif|left|200px]]
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{{Structure
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|RELATEDENTRY=[[1svm|1SVM]], [[1svo|1SVO]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svl OCA], [http://www.ebi.ac.uk/pdbsum/1svl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svl RCSB]</span>
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'''Co-crystal structure of SV40 large T antigen helicase domain and ADP'''
'''Co-crystal structure of SV40 large T antigen helicase domain and ADP'''
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[[Category: Gai, D.]]
[[Category: Gai, D.]]
[[Category: Zhao, R.]]
[[Category: Zhao, R.]]
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[[Category: aaa+ fold]]
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[[Category: Aaa+ fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:11:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:32 2008''
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Revision as of 06:11, 3 May 2008

Image:1svl.gif

Template:STRUCTURE 1svl

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. 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 Sat May 3 09:11:16 2008

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