1vcc: Difference between revisions

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[[Image:1vcc.gif|left|200px]]<br /><applet load="1vcc" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1vcc.gif|left|200px]]<br /><applet load="1vcc" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1vcc, resolution 1.6Å" />

'''AMINO TERMINAL 9KDA DOMAIN OF VACCINIA VIRUS DNA TOPOISOMERASE I RESIDUES 1-77, EXPERIMENTAL ELECTRON DENSITY FOR RESIDUES 1-77'''<br />

==Overview==

BACKGROUND: Vaccinia virus, a cytoplasmically-replicating poxvirus, encodes a type I DNA topoisomerase that is biochemically similar to, eukaryotic-like DNA topoisomerases I, and which has been widely studied as, a model topoisomerase. It is the smallest topoisomerase known and is, unusual in that it is resistant to the potent chemotherapeutic agent, camptothecin. RESULTS: The crystal structure of a 9 kDa amino-terminal, fragment of vaccinia virus DNA topoisomerase I has been determined at 1.6, A resolution. The fragment forms a five-stranded, antiparallel beta-sheet, with two short alpha-helices and connecting loops. Residues that are, conserved between all eukaryotic-like type I topoisomerases are not, clustered in particular regions of the structure. CONCLUSIONS: This is the, first atomic structure of any region of a eukaryotic-like DNA, topoisomerase I. It has provided insights into the structural bases of the, phenotypes of some single-site mutants of the intact topoisomerase. The, structure has enabled us to study the interactions within a well-folded, protein fragment and the camptothecin resistance of the viral, topoisomerase.

BACKGROUND: Vaccinia virus, a cytoplasmically-replicating poxvirus, encodes a type I DNA topoisomerase that is biochemically similar to eukaryotic-like DNA topoisomerases I, and which has been widely studied as a model topoisomerase. It is the smallest topoisomerase known and is unusual in that it is resistant to the potent chemotherapeutic agent camptothecin. RESULTS: The crystal structure of a 9 kDa amino-terminal fragment of vaccinia virus DNA topoisomerase I has been determined at 1.6 A resolution. The fragment forms a five-stranded, antiparallel beta-sheet with two short alpha-helices and connecting loops. Residues that are conserved between all eukaryotic-like type I topoisomerases are not clustered in particular regions of the structure. CONCLUSIONS: This is the first atomic structure of any region of a eukaryotic-like DNA topoisomerase I. It has provided insights into the structural bases of the phenotypes of some single-site mutants of the intact topoisomerase. The structure has enabled us to study the interactions within a well-folded protein fragment and the camptothecin resistance of the viral topoisomerase.

==About this Structure==

1VCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia 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=1VCC OCA].

1VCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia 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=1VCC OCA].

==Reference==

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[[Category: dna binding]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 04:35:~~03 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:45 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1vcc.gif|left|200px]]<br /><applet load="1vcc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1vcc.gif|left|200px]]<br /><applet load="1vcc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1vcc, resolution 1.6&Aring;" />
 '''AMINO TERMINAL 9KDA DOMAIN OF VACCINIA VIRUS DNA TOPOISOMERASE I RESIDUES 1-77, EXPERIMENTAL ELECTRON DENSITY FOR RESIDUES 1-77'''<br />
 ==Overview==
-BACKGROUND: Vaccinia virus, a cytoplasmically-replicating poxvirus, encodes a type I DNA topoisomerase that is biochemically similar to, eukaryotic-like DNA topoisomerases I, and which has been widely studied as, a model topoisomerase. It is the smallest topoisomerase known and is, unusual in that it is resistant to the potent chemotherapeutic agent, camptothecin. RESULTS: The crystal structure of a 9 kDa amino-terminal, fragment of vaccinia virus DNA topoisomerase I has been determined at 1.6, A resolution. The fragment forms a five-stranded, antiparallel beta-sheet, with two short alpha-helices and connecting loops. Residues that are, conserved between all eukaryotic-like type I topoisomerases are not, clustered in particular regions of the structure. CONCLUSIONS: This is the, first atomic structure of any region of a eukaryotic-like DNA, topoisomerase I. It has provided insights into the structural bases of the, phenotypes of some single-site mutants of the intact topoisomerase. The, structure has enabled us to study the interactions within a well-folded, protein fragment and the camptothecin resistance of the viral, topoisomerase.
+BACKGROUND: Vaccinia virus, a cytoplasmically-replicating poxvirus, encodes a type I DNA topoisomerase that is biochemically similar to eukaryotic-like DNA topoisomerases I, and which has been widely studied as a model topoisomerase. It is the smallest topoisomerase known and is unusual in that it is resistant to the potent chemotherapeutic agent camptothecin. RESULTS: The crystal structure of a 9 kDa amino-terminal fragment of vaccinia virus DNA topoisomerase I has been determined at 1.6 A resolution. The fragment forms a five-stranded, antiparallel beta-sheet with two short alpha-helices and connecting loops. Residues that are conserved between all eukaryotic-like type I topoisomerases are not clustered in particular regions of the structure. CONCLUSIONS: This is the first atomic structure of any region of a eukaryotic-like DNA topoisomerase I. It has provided insights into the structural bases of the phenotypes of some single-site mutants of the intact topoisomerase. The structure has enabled us to study the interactions within a well-folded protein fragment and the camptothecin resistance of the viral topoisomerase.
 ==About this Structure==
-VCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia 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=1VCC OCA].
+VCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia 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=1VCC OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: dna binding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:35:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:45 2008''