1cy9: Difference between revisions
New page: left|200px<br /><applet load="1cy9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cy9, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1cy9.gif|left|200px]]<br /><applet load="1cy9" size=" | [[Image:1cy9.gif|left|200px]]<br /><applet load="1cy9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1cy9, resolution 1.80Å" /> | caption="1cy9, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. MONOCLINIC FORM'''<br /> | '''CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. MONOCLINIC FORM'''<br /> | ||
==Overview== | ==Overview== | ||
DNA topoisomerases are the enzymes responsible for maintaining the | DNA topoisomerases are the enzymes responsible for maintaining the topological states of DNA. In order to change the topology of DNA, topoisomerases pass one or two DNA strands through transient single or double strand breaks in the DNA phosphodiester backbone. It has been proposed that both type IA and type II enzymes change conformation dramatically during the reaction cycle in order to accomplish these transformations. In the case of Escherichia coli DNA topoisomerase I, it has been suggested that a 30 kDa fragment moves away from the rest of the protein to create an entrance into the central hole in the protein. Structures of the 30 kDa fragment reveal that indeed this fragment can change conformation significantly. The fragment is composed of two domains, and while the domains themselves remain largely unchanged, their relative arrangement can change dramatically. | ||
==About this Structure== | ==About this Structure== | ||
1CY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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:// | 1CY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1CY9 OCA]. | ||
==Reference== | ==Reference== | ||
Line 20: | Line 20: | ||
[[Category: dna topoisomerase]] | [[Category: dna topoisomerase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:07 2008'' |
Revision as of 13:11, 21 February 2008
|
CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. MONOCLINIC FORM
OverviewOverview
DNA topoisomerases are the enzymes responsible for maintaining the topological states of DNA. In order to change the topology of DNA, topoisomerases pass one or two DNA strands through transient single or double strand breaks in the DNA phosphodiester backbone. It has been proposed that both type IA and type II enzymes change conformation dramatically during the reaction cycle in order to accomplish these transformations. In the case of Escherichia coli DNA topoisomerase I, it has been suggested that a 30 kDa fragment moves away from the rest of the protein to create an entrance into the central hole in the protein. Structures of the 30 kDa fragment reveal that indeed this fragment can change conformation significantly. The fragment is composed of two domains, and while the domains themselves remain largely unchanged, their relative arrangement can change dramatically.
About this StructureAbout this Structure
1CY9 is a Single protein structure of sequence from Escherichia coli. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.
ReferenceReference
Conformational changes in E. coli DNA topoisomerase I., Feinberg H, Lima CD, Mondragon A, Nat Struct Biol. 1999 Oct;6(10):918-22. PMID:10504724
Page seeded by OCA on Thu Feb 21 12:11:07 2008