1CY2
COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH TPTPTP3'
Summary for 1CY2
| Entry DOI | 10.2210/pdb1cy2/pdb |
| Related | 1CY0 1CY1 1CY4 1CY6 1CY7 1CY8 1CY9 1CYY |
| Descriptor | DNA TOPOISOMERASE I, PHOSPHATE ION, THYMIDINE-5'-PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | dna topoisomerase, relaxing enzyme, isomerase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 68281.89 |
| Authors | Feinberg, H.,Changela, A.,Mondragon, A. (deposition date: 1999-08-31, release date: 2000-03-08, Last modification date: 2024-05-22) |
| Primary citation | Feinberg, H.,Changela, A.,Mondragon, A. Protein-nucleotide interactions in E. coli DNA topoisomerase I. Nat.Struct.Biol., 6:961-968, 1999 Cited by PubMed Abstract: DNA topoisomerases are the enzymes responsible for controlling and maintaining the topological states of DNA. Type IA enzymes work by transiently breaking the phosphodiester backbone of one strand to allow passage of another strand through the break. The protein has to perform complex rearrangements of the DNA, and hence it is likely that different regions of the enzyme bind DNA with different affinities. In order to identify some of the DNA binding sites in the protein, we have solved the structures of several complexes of the 67 kDa N-terminal fragment of Escherichia coli DNA topoisomerase I with mono- and trinucleotides. There are five different binding sites in the complexes, one of which is adjacent to the active site. Two other sites are in the central hole of the protein and may represent general DNA binding regions. The positions of these sites allow us to identify different DNA binding regions and to understand their possible roles in the catalytic cycle. PubMed: 10504732DOI: 10.1038/13333 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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