2gaj
From Proteopedia
(New page: 200px<br /><applet load="2gaj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gaj, resolution 1.950Å" /> '''Structure of Full L...) |
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| - | [[Image:2gaj.gif|left|200px]]<br /><applet load="2gaj" size=" | + | [[Image:2gaj.gif|left|200px]]<br /><applet load="2gaj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gaj, resolution 1.950Å" /> | caption="2gaj, resolution 1.950Å" /> | ||
'''Structure of Full Length Topoisomerase I from Thermotoga maritima in monoclinic crystal form'''<br /> | '''Structure of Full Length Topoisomerase I from Thermotoga maritima in monoclinic crystal form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | DNA topoisomerases are a family of enzymes altering the topology of DNA by | + | DNA topoisomerases are a family of enzymes altering the topology of DNA by concerted breakage and rejoining of the phosphodiester backbone of DNA. Bacterial and archeal type IA topoisomerases, including topoisomerase I, topoisomerase III, and reverse gyrase, are crucial in regulation of DNA supercoiling and maintenance of genetic stability. The crystal structure of full length topoisomerase I from Thermotoga maritima was determined at 1.7A resolution and represents an intact and fully active bacterial topoisomerase I. It reveals the torus-like structure of the conserved transesterification core domain comprising domains I-IV and a tightly associated C-terminal zinc ribbon domain (domain V) packing against domain IV of the core domain. The previously established zinc-independence of the functional activity of T.maritima topoisomerase I is further supported by its crystal structure as no zinc ion is bound to domain V. However, the structural integrity is preserved by the formation of two disulfide bridges between the four Zn-binding cysteine residues. A functional role of domain V in DNA binding and recognition is suggested and discussed in the light of the structure and previous biochemical findings. In addition, implications for bacterial topoisomerases I are provided. |
==About this Structure== | ==About this Structure== | ||
| - | 2GAJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. 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:// | + | 2GAJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. 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=2GAJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc ribbon]] | [[Category: zinc ribbon]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:29:48 2008'' |
Revision as of 15:29, 21 February 2008
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Structure of Full Length Topoisomerase I from Thermotoga maritima in monoclinic crystal form
Overview
DNA topoisomerases are a family of enzymes altering the topology of DNA by concerted breakage and rejoining of the phosphodiester backbone of DNA. Bacterial and archeal type IA topoisomerases, including topoisomerase I, topoisomerase III, and reverse gyrase, are crucial in regulation of DNA supercoiling and maintenance of genetic stability. The crystal structure of full length topoisomerase I from Thermotoga maritima was determined at 1.7A resolution and represents an intact and fully active bacterial topoisomerase I. It reveals the torus-like structure of the conserved transesterification core domain comprising domains I-IV and a tightly associated C-terminal zinc ribbon domain (domain V) packing against domain IV of the core domain. The previously established zinc-independence of the functional activity of T.maritima topoisomerase I is further supported by its crystal structure as no zinc ion is bound to domain V. However, the structural integrity is preserved by the formation of two disulfide bridges between the four Zn-binding cysteine residues. A functional role of domain V in DNA binding and recognition is suggested and discussed in the light of the structure and previous biochemical findings. In addition, implications for bacterial topoisomerases I are provided.
About this Structure
2GAJ is a Single protein structure of sequence from Thermotoga maritima. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of full length topoisomerase I from Thermotoga maritima., Hansen G, Harrenga A, Wieland B, Schomburg D, Reinemer P, J Mol Biol. 2006 May 19;358(5):1328-40. Epub 2006 Mar 23. PMID:16600296
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