1nui

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(New page: 200px<br /><applet load="1nui" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nui, resolution 2.90&Aring;" /> '''Crystal Structure of...)
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[[Image:1nui.gif|left|200px]]<br /><applet load="1nui" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nui, resolution 2.90&Aring;" />
caption="1nui, resolution 2.90&Aring;" />
'''Crystal Structure of the primase fragment of Bacteriophage T7 primase-helicase protein'''<br />
'''Crystal Structure of the primase fragment of Bacteriophage T7 primase-helicase protein'''<br />
==Overview==
==Overview==
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DNA primases are template-dependent RNA polymerases that synthesize, oligoribonucleotide primers that can be extended by DNA polymerase. The, bacterial primases consist of zinc binding and RNA polymerase domains that, polymerize ribonucleotides at templating sequences of single-stranded DNA., We report a crystal structure of bacteriophage T7 primase that reveals its, two domains and the presence of two Mg(2+) ions bound to the active site., NMR and biochemical data show that the two domains remain separated until, the primase binds to DNA and nucleotide. The zinc binding domain alone can, stimulate primer extension by T7 DNA polymerase. These findings suggest, that the zinc binding domain couples primer synthesis with primer, utilization by securing the DNA template in the primase active site and, then delivering the primed DNA template to DNA polymerase. The modular, architecture of the primase and a similar mechanism of priming DNA, synthesis are likely to apply broadly to prokaryotic primases.
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DNA primases are template-dependent RNA polymerases that synthesize oligoribonucleotide primers that can be extended by DNA polymerase. The bacterial primases consist of zinc binding and RNA polymerase domains that polymerize ribonucleotides at templating sequences of single-stranded DNA. We report a crystal structure of bacteriophage T7 primase that reveals its two domains and the presence of two Mg(2+) ions bound to the active site. NMR and biochemical data show that the two domains remain separated until the primase binds to DNA and nucleotide. The zinc binding domain alone can stimulate primer extension by T7 DNA polymerase. These findings suggest that the zinc binding domain couples primer synthesis with primer utilization by securing the DNA template in the primase active site and then delivering the primed DNA template to DNA polymerase. The modular architecture of the primase and a similar mechanism of priming DNA synthesis are likely to apply broadly to prokaryotic primases.
==About this Structure==
==About this Structure==
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1NUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] with ZN and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NUI OCA].
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1NUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NUI OCA].
==Reference==
==Reference==
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[[Category: Ito, T.]]
[[Category: Ito, T.]]
[[Category: Kato, M.]]
[[Category: Kato, M.]]
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[[Category: Richardson, C.C.]]
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[[Category: Richardson, C C.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: zinc-biding domain]]
[[Category: zinc-biding domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:33:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:07 2008''

Revision as of 12:10, 21 February 2008


1nui, resolution 2.90Å

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Crystal Structure of the primase fragment of Bacteriophage T7 primase-helicase protein

Overview

DNA primases are template-dependent RNA polymerases that synthesize oligoribonucleotide primers that can be extended by DNA polymerase. The bacterial primases consist of zinc binding and RNA polymerase domains that polymerize ribonucleotides at templating sequences of single-stranded DNA. We report a crystal structure of bacteriophage T7 primase that reveals its two domains and the presence of two Mg(2+) ions bound to the active site. NMR and biochemical data show that the two domains remain separated until the primase binds to DNA and nucleotide. The zinc binding domain alone can stimulate primer extension by T7 DNA polymerase. These findings suggest that the zinc binding domain couples primer synthesis with primer utilization by securing the DNA template in the primase active site and then delivering the primed DNA template to DNA polymerase. The modular architecture of the primase and a similar mechanism of priming DNA synthesis are likely to apply broadly to prokaryotic primases.

About this Structure

1NUI is a Single protein structure of sequence from Bacteriophage t7 with and as ligands. Full crystallographic information is available from OCA.

Reference

Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis., Kato M, Ito T, Wagner G, Richardson CC, Ellenberger T, Mol Cell. 2003 May;11(5):1349-60. PMID:12769857

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