1MW9
Crystal Structure of H365R mutant of 67 kDA N-terminal fragment of E. coli DNA Topoisomerase I
Summary for 1MW9
| Entry DOI | 10.2210/pdb1mw9/pdb |
| Related | 1ECL 1MW8 |
| Descriptor | DNA Topoisomerase I, SULFATE ION (3 entities in total) |
| Functional Keywords | dna topoisomerase, decatenase enzyme, toprim domain, isomerase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 67795.38 |
| Authors | Perry, K.,Mondragon, A. (deposition date: 2002-09-27, release date: 2003-10-14, Last modification date: 2024-02-14) |
| Primary citation | Perry, K.,Mondragon, A. Structure of a Complex between E. coli DNA Topoisomerase I and Single-Stranded DNA. Structure, 11:1349-1358, 2003 Cited by PubMed Abstract: In order to gain insights into the mechaism of ssDNA binding and recognition by Escherichia coli DNA topoisomerase I, the structure of the 67 kDa N-terminal fragment of topoisomerase I was solved in complex with ssDNA. The structure reveals a new conformational stage in the multistep catalytic cycle of type IA topoisomerases. In the structure, the ssDNA binding groove leading to the active site is occupied, but the active site is not fully formed. Large conformational changes are not seen; instead, a single helix parallel to the ssDNA binding groove shifts to clamp the ssDNA. The structure helps clarify the temporal sequence of conformational events, starting from an initial empty enzyme and proceeding to a ssDNA-occupied and catalytically competent active site. PubMed: 14604525DOI: 10.1016/j.str.2003.09.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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