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| [[Image:1q57.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1q57| PDB=1q57 | SCENE= }} | | {{STRUCTURE_1q57| PDB=1q57 | SCENE= }} |
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| '''The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7'''
| | ===The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7=== |
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| ==Overview==
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| Within minutes after infecting Escherichia coli, bacteriophage T7 synthesizes many copies of its genomic DNA. The lynchpin of the T7 replication system is a bifunctional primase-helicase that unwinds duplex DNA at the replication fork while initiating the synthesis of Okazaki fragments on the lagging strand. We have determined a 3.45 A crystal structure of the T7 primase-helicase that shows an articulated arrangement of the primase and helicase sites. The crystallized primase-helicase is a heptamer with a crown-like shape, reflecting an intimate packing of helicase domains into a ring that is topped with loosely arrayed primase domains. This heptameric isoform can accommodate double-stranded DNA in its central channel, which nicely explains its recently described DNA remodeling activity. The double-jointed structure of the primase-helicase permits a free range of motion for the primase and helicase domains that suggests how the continuous unwinding of DNA at the replication fork can be periodically coupled to Okazaki fragment synthesis.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14636571}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14636571 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14636571}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Helicase]] | | [[Category: Helicase]] |
| [[Category: Primase]] | | [[Category: Primase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:52:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:32:06 2008'' |
