1z8s

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(New page: 200px<br /><applet load="1z8s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z8s" /> '''DnaB binding domain of DnaG (P16) from Bacil...)
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[[Image:1z8s.gif|left|200px]]<br /><applet load="1z8s" size="350" color="white" frame="true" align="right" spinBox="true"
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'''DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)'''<br />
'''DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)'''<br />
==Overview==
==Overview==
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The helicase-primase interaction is a critical event in DNA replication, and is mediated by a putative helicase-interaction domain within the, primase. The solution structure of the helicase-interaction domain of DnaG, reveals that it is made up of two independent subdomains: an N-terminal, six-helix module and a C-terminal two-helix module that contains the, residues of the primase previously identified as important in the, interaction with the helicase. We show that the two-helix module alone is, sufficient for strong binding between the primase and the helicase but, fails to activate the helicase; both subdomains are required for helicase, activation. The six-helix module of the primase has only one close, structural homolog, the N-terminal domain of the corresponding helicase., This surprising structural relationship, coupled with the differences in, surface properties of the two molecules, suggests how the, helicase-interaction domain may perturb the structure of the helicase and, lead to activation.
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The helicase-primase interaction is a critical event in DNA replication and is mediated by a putative helicase-interaction domain within the primase. The solution structure of the helicase-interaction domain of DnaG reveals that it is made up of two independent subdomains: an N-terminal six-helix module and a C-terminal two-helix module that contains the residues of the primase previously identified as important in the interaction with the helicase. We show that the two-helix module alone is sufficient for strong binding between the primase and the helicase but fails to activate the helicase; both subdomains are required for helicase activation. The six-helix module of the primase has only one close structural homolog, the N-terminal domain of the corresponding helicase. This surprising structural relationship, coupled with the differences in surface properties of the two molecules, suggests how the helicase-interaction domain may perturb the structure of the helicase and lead to activation.
==About this Structure==
==About this Structure==
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1Z8S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z8S OCA].
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1Z8S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z8S OCA].
==Reference==
==Reference==
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hounslow, A.M.]]
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[[Category: Hounslow, A M.]]
[[Category: Soultanas, P.]]
[[Category: Soultanas, P.]]
[[Category: Syson, K.]]
[[Category: Syson, K.]]
[[Category: Thirlway, J.]]
[[Category: Thirlway, J.]]
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[[Category: Waltho, J.P.]]
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[[Category: Waltho, J P.]]
[[Category: two alpha helical sub-domains]]
[[Category: two alpha helical sub-domains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:18:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:10 2008''

Revision as of 14:13, 21 February 2008


1z8s

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DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)

Overview

The helicase-primase interaction is a critical event in DNA replication and is mediated by a putative helicase-interaction domain within the primase. The solution structure of the helicase-interaction domain of DnaG reveals that it is made up of two independent subdomains: an N-terminal six-helix module and a C-terminal two-helix module that contains the residues of the primase previously identified as important in the interaction with the helicase. We show that the two-helix module alone is sufficient for strong binding between the primase and the helicase but fails to activate the helicase; both subdomains are required for helicase activation. The six-helix module of the primase has only one close structural homolog, the N-terminal domain of the corresponding helicase. This surprising structural relationship, coupled with the differences in surface properties of the two molecules, suggests how the helicase-interaction domain may perturb the structure of the helicase and lead to activation.

About this Structure

1Z8S is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation., Syson K, Thirlway J, Hounslow AM, Soultanas P, Waltho JP, Structure. 2005 Apr;13(4):609-16. PMID:15837199

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