1oyy

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(New page: 200px<br /><applet load="1oyy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oyy, resolution 2.5&Aring;" /> '''Structure of the RecQ...)
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[[Image:1oyy.jpg|left|200px]]<br /><applet load="1oyy" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oyy.jpg|left|200px]]<br /><applet load="1oyy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oyy, resolution 2.5&Aring;" />
caption="1oyy, resolution 2.5&Aring;" />
'''Structure of the RecQ Catalytic Core bound to ATP-gamma-S'''<br />
'''Structure of the RecQ Catalytic Core bound to ATP-gamma-S'''<br />
==Overview==
==Overview==
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RecQ family helicases catalyze critical genome maintenance reactions in, bacterial and eukaryotic cells, playing key roles in several DNA metabolic, processes. Mutations in recQ genes are linked to genome instability and, human disease. To define the physical basis of RecQ enzyme function, we, have determined a 1.8 A resolution crystal structure of the catalytic core, of Escherichia coli RecQ in its unbound form and a 2.5 A resolution, structure of the core bound to the ATP analog ATPgammaS. The RecQ core, comprises four conserved subdomains; two of these combine to form its, helicase region, while the others form unexpected Zn(2+)-binding and, winged-helix motifs. The structures reveal the molecular basis of missense, mutations that cause Bloom's syndrome, a human RecQ-associated disease., Finally, based on findings from the structures, we propose a mechanism for, RecQ activity that could explain its functional coordination with, topoisomerase III.
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RecQ family helicases catalyze critical genome maintenance reactions in bacterial and eukaryotic cells, playing key roles in several DNA metabolic processes. Mutations in recQ genes are linked to genome instability and human disease. To define the physical basis of RecQ enzyme function, we have determined a 1.8 A resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of the core bound to the ATP analog ATPgammaS. The RecQ core comprises four conserved subdomains; two of these combine to form its helicase region, while the others form unexpected Zn(2+)-binding and winged-helix motifs. The structures reveal the molecular basis of missense mutations that cause Bloom's syndrome, a human RecQ-associated disease. Finally, based on findings from the structures, we propose a mechanism for RecQ activity that could explain its functional coordination with topoisomerase III.
==About this Structure==
==About this Structure==
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1OYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, MN and AGS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OYY OCA].
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1OYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=AGS:'>AGS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYY OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bernstein, D.A.]]
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[[Category: Bernstein, D A.]]
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[[Category: Keck, J.L.]]
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[[Category: Keck, J L.]]
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[[Category: Zittel, M.C.]]
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[[Category: Zittel, M C.]]
[[Category: AGS]]
[[Category: AGS]]
[[Category: MN]]
[[Category: MN]]
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[[Category: zn(2+) binding]]
[[Category: zn(2+) binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:18:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:15 2008''

Revision as of 12:23, 21 February 2008

Image:1oyy.jpg

1oyy, resolution 2.5Å

Drag the structure with the mouse to rotate

Structure of the RecQ Catalytic Core bound to ATP-gamma-S

Overview

RecQ family helicases catalyze critical genome maintenance reactions in bacterial and eukaryotic cells, playing key roles in several DNA metabolic processes. Mutations in recQ genes are linked to genome instability and human disease. To define the physical basis of RecQ enzyme function, we have determined a 1.8 A resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of the core bound to the ATP analog ATPgammaS. The RecQ core comprises four conserved subdomains; two of these combine to form its helicase region, while the others form unexpected Zn(2+)-binding and winged-helix motifs. The structures reveal the molecular basis of missense mutations that cause Bloom's syndrome, a human RecQ-associated disease. Finally, based on findings from the structures, we propose a mechanism for RecQ activity that could explain its functional coordination with topoisomerase III.

About this Structure

1OYY is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

Reference

High-resolution structure of the E.coli RecQ helicase catalytic core., Bernstein DA, Zittel MC, Keck JL, EMBO J. 2003 Oct 1;22(19):4910-21. PMID:14517231

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