1svo
From Proteopedia
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'''Structure of SV40 large T antigen helicase domain''' | '''Structure of SV40 large T antigen helicase domain''' | ||
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[[Category: Gai, D.]] | [[Category: Gai, D.]] | ||
[[Category: Zhao, R.]] | [[Category: Zhao, R.]] | ||
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Revision as of 06:11, 3 May 2008
Structure of SV40 large T antigen helicase domain
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
1SVO 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 09:11:29 2008
