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| [[Image:1svl.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1svl| PDB=1svl | SCENE= }} | | {{STRUCTURE_1svl| PDB=1svl | SCENE= }} |
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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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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15454080}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15454080 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15454080}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zhao, R.]] | | [[Category: Zhao, R.]] |
| [[Category: Aaa+ fold]] | | [[Category: Aaa+ fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:11:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:21:58 2008'' |
