2h7g

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(New page: 200px<br /><applet load="2h7g" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h7g, resolution 1.900&Aring;" /> '''Structure of variol...)
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[[Image:2h7g.gif|left|200px]]<br /><applet load="2h7g" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2h7g.gif|left|200px]]<br /><applet load="2h7g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2h7g, resolution 1.900&Aring;" />
caption="2h7g, resolution 1.900&Aring;" />
'''Structure of variola topoisomerase non-covalently bound to DNA'''<br />
'''Structure of variola topoisomerase non-covalently bound to DNA'''<br />
==Overview==
==Overview==
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Although smallpox has been eradicated from the human population, it is, presently feared as a possible agent of bioterrorism. The smallpox virus, codes for its own topoisomerase enzyme that differs from its cellular, counterpart by requiring a specific DNA sequence for activation of, catalysis. Here we present crystal structures of the smallpox virus, topoisomerase enzyme bound both covalently and noncovalently to a specific, DNA sequence. These structures reveal the basis for site-specific DNA, recognition, and they explain how catalysis is likely activated by, formation of a specific enzyme-DNA interface. Unexpectedly, the poxvirus, enzyme uses a major groove binding alpha helix that is not present in the, human enzyme to recognize part of the core recognition sequence and, activate the enzyme for catalysis. The topoisomerase-DNA complex, structures also provide a three-dimensional framework that may facilitate, the rational design of therapeutic agents to treat poxvirus infections.
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Although smallpox has been eradicated from the human population, it is presently feared as a possible agent of bioterrorism. The smallpox virus codes for its own topoisomerase enzyme that differs from its cellular counterpart by requiring a specific DNA sequence for activation of catalysis. Here we present crystal structures of the smallpox virus topoisomerase enzyme bound both covalently and noncovalently to a specific DNA sequence. These structures reveal the basis for site-specific DNA recognition, and they explain how catalysis is likely activated by formation of a specific enzyme-DNA interface. Unexpectedly, the poxvirus enzyme uses a major groove binding alpha helix that is not present in the human enzyme to recognize part of the core recognition sequence and activate the enzyme for catalysis. The topoisomerase-DNA complex structures also provide a three-dimensional framework that may facilitate the rational design of therapeutic agents to treat poxvirus infections.
==About this Structure==
==About this Structure==
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2H7G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Variola_virus Variola virus]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H7G OCA].
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2H7G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Variola_virus Variola virus]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7G OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Variola virus]]
[[Category: Variola virus]]
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[[Category: Bushman, F.D.]]
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[[Category: Bushman, F D.]]
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[[Category: Duyne, G.D.Van.]]
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[[Category: Duyne, G D.Van.]]
[[Category: Hwang, Y.]]
[[Category: Hwang, Y.]]
[[Category: Perry, K.]]
[[Category: Perry, K.]]
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[[Category: type ib topoisomerase]]
[[Category: type ib topoisomerase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:35:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:38:58 2008''

Revision as of 15:38, 21 February 2008


2h7g, resolution 1.900Å

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Structure of variola topoisomerase non-covalently bound to DNA

Overview

Although smallpox has been eradicated from the human population, it is presently feared as a possible agent of bioterrorism. The smallpox virus codes for its own topoisomerase enzyme that differs from its cellular counterpart by requiring a specific DNA sequence for activation of catalysis. Here we present crystal structures of the smallpox virus topoisomerase enzyme bound both covalently and noncovalently to a specific DNA sequence. These structures reveal the basis for site-specific DNA recognition, and they explain how catalysis is likely activated by formation of a specific enzyme-DNA interface. Unexpectedly, the poxvirus enzyme uses a major groove binding alpha helix that is not present in the human enzyme to recognize part of the core recognition sequence and activate the enzyme for catalysis. The topoisomerase-DNA complex structures also provide a three-dimensional framework that may facilitate the rational design of therapeutic agents to treat poxvirus infections.

About this Structure

2H7G is a Single protein structure of sequence from Variola virus. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.

Reference

Structural basis for specificity in the poxvirus topoisomerase., Perry K, Hwang Y, Bushman FD, Van Duyne GD, Mol Cell. 2006 Aug 4;23(3):343-54. PMID:16885024

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