Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.3
Classification:ISOMERASE
Release Date:2006-01-31
Deposition Date:2005-05-21
Revision Date:2008-04-30#2011-07-13#2017-10-11
Molecular Weight:120686.88
Macromolecule Type:Protein
Residue Count:1038
Atom Site Count:8510
DOI:10.2210/pdb2csb/pdb
Abstract:
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.
Resolution:2.3
Classification:ISOMERASE
Release Date:2006-01-31
Deposition Date:2005-05-21
Revision Date:2008-04-30#2011-07-13#2017-10-11
Molecular Weight:120686.88
Macromolecule Type:Protein
Residue Count:1038
Atom Site Count:8510
DOI:10.2210/pdb2csb/pdb
Abstract:
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.
| Date made available | 2006 |
|---|---|
| Publisher | RCSB-PDB |