1e0j

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(New page: 200px<br /><applet load="1e0j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e0j, resolution 3.00&Aring;" /> '''GP4D HELICASE FROM P...)
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[[Image:1e0j.jpg|left|200px]]<br /><applet load="1e0j" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1e0j, resolution 3.00&Aring;" />
caption="1e0j, resolution 3.00&Aring;" />
'''GP4D HELICASE FROM PHAGE T7 ADPNP COMPLEX'''<br />
'''GP4D HELICASE FROM PHAGE T7 ADPNP COMPLEX'''<br />
==Overview==
==Overview==
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We have determined the crystal structure of an active, hexameric fragment, of the gene 4 helicase from bacteriophage T7. The structure reveals how, subunit contacts stabilize the hexamer. Deviation from expected six-fold, symmetry of the hexamer indicates that the structure is of an intermediate, on the catalytic pathway. The structural consequences of the asymmetry, suggest a "binding change" mechanism to explain how cooperative binding, and hydrolysis of nucleotides are coupled to conformational changes in the, ring that most likely accompany duplex unwinding. The structure of a, complex with a nonhydrolyzable ATP analog provides additional evidence for, this hypothesis, with only four of the six possible nucleotide binding, sites being occupied in this conformation of the hexamer. This model, suggests a mechanism for DNA translocation.
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We have determined the crystal structure of an active, hexameric fragment of the gene 4 helicase from bacteriophage T7. The structure reveals how subunit contacts stabilize the hexamer. Deviation from expected six-fold symmetry of the hexamer indicates that the structure is of an intermediate on the catalytic pathway. The structural consequences of the asymmetry suggest a "binding change" mechanism to explain how cooperative binding and hydrolysis of nucleotides are coupled to conformational changes in the ring that most likely accompany duplex unwinding. The structure of a complex with a nonhydrolyzable ATP analog provides additional evidence for this hypothesis, with only four of the six possible nucleotide binding sites being occupied in this conformation of the hexamer. This model suggests a mechanism for DNA translocation.
==About this Structure==
==About this Structure==
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1E0J 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 MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E0J OCA].
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1E0J 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=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0J OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger, T.]]
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[[Category: Sawaya, M.R.]]
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[[Category: Sawaya, M R.]]
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[[Category: Singleton, M.R.]]
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[[Category: Singleton, M R.]]
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[[Category: Wigley, D.B.]]
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[[Category: Wigley, D B.]]
[[Category: ANP]]
[[Category: ANP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: helicase]]
[[Category: helicase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:42:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:31 2008''

Revision as of 10:22, 21 February 2008

Image:1e0j.jpg

1e0j, resolution 3.00Å

Drag the structure with the mouse to rotate

GP4D HELICASE FROM PHAGE T7 ADPNP COMPLEX

Overview

We have determined the crystal structure of an active, hexameric fragment of the gene 4 helicase from bacteriophage T7. The structure reveals how subunit contacts stabilize the hexamer. Deviation from expected six-fold symmetry of the hexamer indicates that the structure is of an intermediate on the catalytic pathway. The structural consequences of the asymmetry suggest a "binding change" mechanism to explain how cooperative binding and hydrolysis of nucleotides are coupled to conformational changes in the ring that most likely accompany duplex unwinding. The structure of a complex with a nonhydrolyzable ATP analog provides additional evidence for this hypothesis, with only four of the six possible nucleotide binding sites being occupied in this conformation of the hexamer. This model suggests a mechanism for DNA translocation.

About this Structure

1E0J is a Single protein structure of sequence from Bacteriophage t7 with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides., Singleton MR, Sawaya MR, Ellenberger T, Wigley DB, Cell. 2000 Jun 9;101(6):589-600. PMID:10892646

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