1a36
From Proteopedia
(New page: 200px<br /> <applet load="1a36" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a36, resolution 2.800Å" /> '''TOPOISOMERASE I/DN...) |
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| - | [[Image:1a36.gif|left|200px]]<br /> | + | [[Image:1a36.gif|left|200px]]<br /><applet load="1a36" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a36" size=" | + | |
caption="1a36, resolution 2.800Å" /> | caption="1a36, resolution 2.800Å" /> | ||
'''TOPOISOMERASE I/DNA COMPLEX'''<br /> | '''TOPOISOMERASE I/DNA COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of a 70-kilodalton amino terminally | + | The three-dimensional structure of a 70-kilodalton amino terminally truncated form of human topoisomerase I in complex with a 22-base pair duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact DNA. The linker region that connects the central core of the enzyme to the carboxyl-terminal domain assumes a coiled-coil configuration and protrudes away from the remainder of the enzyme. The positively charged DNA-proximal surface of the linker makes only a few contacts with the DNA downstream of the cleavage site. In combination with the crystal structures of the reconstituted human topoisomerase I before and after DNA cleavage, this information suggests which amino acid residues are involved in catalyzing phosphodiester bond breakage and religation. The structures also lead to the proposal that the topoisomerization step occurs by a mechanism termed "controlled rotation." |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A36 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1A36 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb73_1.html Topoisomerases]]. 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:// | + | 1A36 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1A36 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb73_1.html Topoisomerases]]. 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=1A36 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Topoisomerases]] | [[Category: Topoisomerases]] | ||
| - | [[Category: Champoux, J | + | [[Category: Champoux, J J.]] |
| - | [[Category: Hol, W | + | [[Category: Hol, W G.J.]] |
[[Category: Qiu, X.]] | [[Category: Qiu, X.]] | ||
| - | [[Category: Redinbo, M | + | [[Category: Redinbo, M R.]] |
[[Category: Stewart, L.]] | [[Category: Stewart, L.]] | ||
[[Category: complex (isomerase/dna)]] | [[Category: complex (isomerase/dna)]] | ||
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[[Category: topoisomerase i]] | [[Category: topoisomerase i]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:18 2008'' |
Revision as of 09:40, 21 February 2008
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TOPOISOMERASE I/DNA COMPLEX
Contents |
Overview
The three-dimensional structure of a 70-kilodalton amino terminally truncated form of human topoisomerase I in complex with a 22-base pair duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact DNA. The linker region that connects the central core of the enzyme to the carboxyl-terminal domain assumes a coiled-coil configuration and protrudes away from the remainder of the enzyme. The positively charged DNA-proximal surface of the linker makes only a few contacts with the DNA downstream of the cleavage site. In combination with the crystal structures of the reconstituted human topoisomerase I before and after DNA cleavage, this information suggests which amino acid residues are involved in catalyzing phosphodiester bond breakage and religation. The structures also lead to the proposal that the topoisomerization step occurs by a mechanism termed "controlled rotation."
Disease
Known disease associated with this structure: DNA topoisomerase I, camptothecin-resistant OMIM:[126420]
About this Structure
1A36 is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1A36 with [Topoisomerases]. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.
Reference
A model for the mechanism of human topoisomerase I., Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ, Science. 1998 Mar 6;279(5356):1534-41. PMID:9488652
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