3M6K
Crystal Structure of N-terminal 44 kDa fragment of topoisomerase V in the presence of guanidium hydrochloride
Summary for 3M6K
| Entry DOI | 10.2210/pdb3m6k/pdb |
| Descriptor | Topoisomerase V, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | helix-hairpin-helix, topoisomerase, conformational change in protein, isomerase, guanidium hydrochloride |
| Biological source | Methanopyrus kandleri |
| Total number of polymer chains | 2 |
| Total formula weight | 88748.94 |
| Authors | Rajan, R.,Taneja, B.,Mondragon, A. (deposition date: 2010-03-15, release date: 2010-08-04, Last modification date: 2011-07-13) |
| Primary citation | Rajan, R.,Taneja, B.,Mondragon, A. Structures of minimal catalytic fragments of topoisomerase v reveals conformational changes relevant for DNA binding. Structure, 18:829-838, 2010 Cited by PubMed Abstract: Topoisomerase V is an archaeal type I topoisomerase that is unique among topoisomerases due to presence of both topoisomerase and DNA repair activities in the same protein. It is organized as an N-terminal topoisomerase domain followed by 24 tandem helix-hairpin-helix (HhH) motifs. Structural studies have shown that the active site is buried by the (HhH) motifs. Here we show that the N-terminal domain can relax DNA in the absence of any HhH motifs and that the HhH motifs are required for stable protein-DNA complex formation. Crystal structures of various topoisomerase V fragments show changes in the relative orientation of the domains mediated by a long bent linker helix, and these movements are essential for the DNA to enter the active site. Phosphate ions bound to the protein near the active site helped model DNA in the topoisomerase domain and show how topoisomerase V may interact with DNA. PubMed: 20637419DOI: 10.1016/j.str.2010.03.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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