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1svo
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(New page: 200px<br /><applet load="1svo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1svo, resolution 2.6Å" /> '''Structure of SV40 lar...)
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Revision as of 00:38, 21 November 2007
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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 with ZN as ligand. 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 Wed Nov 21 02:45:59 2007
