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| [[Image:1fou.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1fou| PDB=1fou | SCENE= }} | | {{STRUCTURE_1fou| PDB=1fou | SCENE= }} |
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| '''CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29'''
| | ===CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29=== |
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| ==Overview==
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| Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head-prohead RNA-ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11130079}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11130079 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11130079}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tao, Y.]] | | [[Category: Tao, Y.]] |
| [[Category: Alpha-helical barrel]] | | [[Category: Alpha-helical barrel]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:35:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:42:17 2008'' |
