1a41

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(New page: 200px<br /><applet load="1a41" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a41, resolution 2.3&Aring;" /> '''TYPE 1-TOPOISOMERASE ...)
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[[Image:1a41.gif|left|200px]]<br /><applet load="1a41" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a41.gif|left|200px]]<br /><applet load="1a41" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1a41, resolution 2.3&Aring;" />
caption="1a41, resolution 2.3&Aring;" />
'''TYPE 1-TOPOISOMERASE CATALYTIC FRAGMENT FROM VACCINIA VIRUS'''<br />
'''TYPE 1-TOPOISOMERASE CATALYTIC FRAGMENT FROM VACCINIA VIRUS'''<br />
==Overview==
==Overview==
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Vaccinia DNA topoisomerase breaks and rejoins DNA strands through a, DNA-(3'-phosphotyrosyl)-enzyme intermediate. A C-terminal catalytic, domain, Topo(81-314), suffices for transesterification chemistry. The, domain contains a constellation of five amino acids, conserved in all, eukaryotic type IB topoisomerases, that catalyzes attack of the tyrosine, nucleophile on the scissile phosphate. The structure of the catalytic, domain, consisting of ten alpha helices and a three-strand beta sheet, resembles the catalytic domains of site-specific recombinases that act via, a topoisomerase IB-like mechanism. The topoisomerase catalytic pentad is, conserved in the tertiary structures of the recombinases despite scant, sequence similarity overall. This implies that the catalytic domains of, type IB topoisomerases and recombinases derive from a common ancestral, strand transferase.
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Vaccinia DNA topoisomerase breaks and rejoins DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate. A C-terminal catalytic domain, Topo(81-314), suffices for transesterification chemistry. The domain contains a constellation of five amino acids, conserved in all eukaryotic type IB topoisomerases, that catalyzes attack of the tyrosine nucleophile on the scissile phosphate. The structure of the catalytic domain, consisting of ten alpha helices and a three-strand beta sheet, resembles the catalytic domains of site-specific recombinases that act via a topoisomerase IB-like mechanism. The topoisomerase catalytic pentad is conserved in the tertiary structures of the recombinases despite scant sequence similarity overall. This implies that the catalytic domains of type IB topoisomerases and recombinases derive from a common ancestral strand transferase.
==About this Structure==
==About this Structure==
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1A41 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1A41 OCA].
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1A41 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1A41 OCA].
==Reference==
==Reference==
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[[Category: type 1b topoisomerase]]
[[Category: type 1b topoisomerase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:35:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:39 2008''

Revision as of 09:40, 21 February 2008


1a41, resolution 2.3Å

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TYPE 1-TOPOISOMERASE CATALYTIC FRAGMENT FROM VACCINIA VIRUS

Overview

Vaccinia DNA topoisomerase breaks and rejoins DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate. A C-terminal catalytic domain, Topo(81-314), suffices for transesterification chemistry. The domain contains a constellation of five amino acids, conserved in all eukaryotic type IB topoisomerases, that catalyzes attack of the tyrosine nucleophile on the scissile phosphate. The structure of the catalytic domain, consisting of ten alpha helices and a three-strand beta sheet, resembles the catalytic domains of site-specific recombinases that act via a topoisomerase IB-like mechanism. The topoisomerase catalytic pentad is conserved in the tertiary structures of the recombinases despite scant sequence similarity overall. This implies that the catalytic domains of type IB topoisomerases and recombinases derive from a common ancestral strand transferase.

About this Structure

1A41 is a Single protein structure of sequence from Vaccinia virus with as ligand. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.

Reference

Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases., Cheng C, Kussie P, Pavletich N, Shuman S, Cell. 1998 Mar 20;92(6):841-50. PMID:9529259

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