2CSD
Crystal structure of Topoisomerase V (61 kDa fragment)
Summary for 2CSD
| Entry DOI | 10.2210/pdb2csd/pdb |
| Related | 2CSB |
| Descriptor | Topoisomerase V (1 entity in total) |
| Functional Keywords | topoisomerase ib, topoisomerase v, helix-turn-helix, helix-hairpin-helix, hhh motif, three helix bundle, isomerase |
| Biological source | Methanopyrus kandleri |
| Total number of polymer chains | 2 |
| Total formula weight | 120006.03 |
| Authors | Taneja, B.,Patel, A.,Slesarev, A.,Mondragon, A. (deposition date: 2005-05-21, release date: 2006-01-31, Last modification date: 2024-11-06) |
| Primary citation | Taneja, B.,Patel, A.,Slesarev, A.,Mondragon, A. Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases Embo J., 25:398-408, 2006 Cited by PubMed 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. PubMed: 16395333DOI: 10.1038/sj.emboj.7600922 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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