2csd
From Proteopedia
(New page: 200px<br /><applet load="2csd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2csd, resolution 2.90Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Topoisomerases are involved in controlling and maintaining the topology of | + | Topoisomerases are involved in controlling and maintaining the topology of DNA and are present in all kingdoms of life. Unlike all other types of topoisomerases, similar type IB enzymes have only been identified in bacteria and eukarya. The only putative type IB topoisomerase in archaea is represented by Methanopyrus kandleri topoisomerase V. Despite several common functional characteristics, topoisomerase V shows no sequence similarity to other members of the same type. The structure of the 61 kDa N-terminal fragment of topoisomerase V reveals no structural similarity to other topoisomerases. Furthermore, the structure of the active site region is different, suggesting no conservation in the cleavage and religation mechanism. Additionally, the active site is buried, indicating the need of a conformational change for activity. The presence of a topoisomerase in archaea with a unique structure suggests the evolution of a separate mechanism to alter DNA. |
==About this Structure== | ==About this Structure== | ||
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[[Category: topoisomerase v]] | [[Category: topoisomerase v]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:51:55 2008'' |
Revision as of 14:51, 21 February 2008
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Crystal structure of Topoisomerase V (61 kDa fragment)
Overview
Topoisomerases are involved in controlling and maintaining the topology of DNA and are present in all kingdoms of life. Unlike all other types of topoisomerases, similar type IB enzymes have only been identified in bacteria and eukarya. The only putative type IB topoisomerase in archaea is represented by Methanopyrus kandleri topoisomerase V. Despite several common functional characteristics, topoisomerase V shows no sequence similarity to other members of the same type. The structure of the 61 kDa N-terminal fragment of topoisomerase V reveals no structural similarity to other topoisomerases. Furthermore, the structure of the active site region is different, suggesting no conservation in the cleavage and religation mechanism. Additionally, the active site is buried, indicating the need of a conformational change for activity. The presence of a topoisomerase in archaea with a unique structure suggests the evolution of a separate mechanism to alter DNA.
About this Structure
2CSD is a Single protein structure of sequence from Methanopyrus kandleri. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases., Taneja B, Patel A, Slesarev A, Mondragon A, EMBO J. 2006 Jan 25;25(2):398-408. Epub 2006 Jan 5. PMID:16395333
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