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| [[Image:2v9p.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2v9p| PDB=2v9p | SCENE= }} | | {{STRUCTURE_2v9p| PDB=2v9p | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF PAPILLOMAVIRUS E1 HEXAMERIC HELICASE DNA-FREE FORM'''
| | ===CRYSTAL STRUCTURE OF PAPILLOMAVIRUS E1 HEXAMERIC HELICASE DNA-FREE FORM=== |
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| ==Overview==
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| Concerted, stochastic and sequential mechanisms of action have been proposed for different hexameric AAA+ molecular motors. Here we report the crystal structure of the E1 helicase from bovine papillomavirus, where asymmetric assembly is for the first time observed in the absence of nucleotide cofactors and DNA. Surprisingly, the ATP-binding sites adopt specific conformations linked to positional changes in the DNA-binding hairpins, which follow a wave-like trajectory, as observed previously in the E1/DNA/ADP complex. The protein's assembly thus maintains such an asymmetric state in the absence of DNA and nucleotide cofactors, allowing consideration of the E1 helicase action as the propagation of a conformational wave around the protein ring. The data imply that the wave's propagation within the AAA+ domains is not necessarily coupled with a strictly sequential hydrolysis of ATP. Since a single ATP hydrolysis event would affect the whole hexamer, such events may simply serve to rectify the direction of the wave's motion.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17881379}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17881379 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17881379}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nucleus]] | | [[Category: Nucleus]] |
| [[Category: Replication]] | | [[Category: Replication]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:26:44 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:30:51 2008'' |
