1q57

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(New page: 200px<br /><applet load="1q57" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q57, resolution 3.45&Aring;" /> '''The Crystal Structur...)
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[[Image:1q57.jpg|left|200px]]<br /><applet load="1q57" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q57, resolution 3.45&Aring;" />
caption="1q57, resolution 3.45&Aring;" />
'''The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7'''<br />
'''The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1Q57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q57 OCA].
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1Q57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q57 OCA].
==Reference==
==Reference==
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[[Category: Ellenberger, T.]]
[[Category: Ellenberger, T.]]
[[Category: Li, Y.]]
[[Category: Li, Y.]]
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[[Category: Sawaya, M.R.]]
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[[Category: Sawaya, M R.]]
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[[Category: Toth, E.A.]]
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[[Category: Toth, E A.]]
[[Category: dna replication]]
[[Category: dna replication]]
[[Category: dntpase]]
[[Category: dntpase]]
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[[Category: primase]]
[[Category: primase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:23:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:57 2008''

Revision as of 12:35, 21 February 2008


1q57, resolution 3.45Å

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The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7

Overview

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.

About this Structure

1Q57 is a Single protein structure of sequence from Bacteriophage t7. Full crystallographic information is available from OCA.

Reference

The crystal structure of the bifunctional primase-helicase of bacteriophage T7., Toth EA, Li Y, Sawaya MR, Cheng Y, Ellenberger T, Mol Cell. 2003 Nov;12(5):1113-23. PMID:14636571

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