2Q2E
Crystal structure of the topoisomerase VI holoenzyme from Methanosarcina mazei
Summary for 2Q2E
| Entry DOI | 10.2210/pdb2q2e/pdb |
| Descriptor | Type II DNA topoisomerase VI subunit A, Type 2 DNA topoisomerase 6 subunit B (2 entities in total) |
| Functional Keywords | topoisomerase, dna-binding, spo11, atpase, isomerase |
| Biological source | Methanosarcina mazei More |
| Total number of polymer chains | 2 |
| Total formula weight | 111032.66 |
| Authors | Corbett, K.D.,Benedetti, P.,Berger, J.M. (deposition date: 2007-05-28, release date: 2007-07-10, Last modification date: 2024-02-21) |
| Primary citation | Corbett, K.D.,Benedetti, P.,Berger, J.M. Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI Nat.Struct.Mol.Biol., 14:611-619, 2007 Cited by PubMed Abstract: Type II topoisomerases help disentangle chromosomes to facilitate cell division. To advance understanding of the structure and dynamics of these essential enzymes, we have determined the crystal structure of an archaeal type IIB topoisomerase, topo VI, at 4.0-A resolution. The 220-kDa heterotetramer adopts a 'twin-gate' architecture, in which a pair of ATPase domains at one end of the enzyme is poised to coordinate DNA movements into the enzyme and through a set of DNA-cleaving domains at the other end. Small-angle X-ray scattering studies show that nucleotide binding elicits a major structural reorganization that is propagated to the enzyme's DNA-cleavage center, explaining how ATP is coupled to DNA capture and strand scission. These data afford important insights into the mechanisms of topo VI and related proteins, including type IIA topoisomerases and the Spo11 meiotic recombination endonuclease. PubMed: 17603498DOI: 10.1038/nsmb1264 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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