1OIS
YEAST DNA TOPOISOMERASE I, N-TERMINAL FRAGMENT
Summary for 1OIS
Entry DOI | 10.2210/pdb1ois/pdb |
Descriptor | DNA TOPOISOMERASE I (2 entities in total) |
Functional Keywords | isomerase, topoisomerase, dna-binding protein, dna binding protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Nucleus, nucleolus: P04786 |
Total number of polymer chains | 1 |
Total formula weight | 26085.76 |
Authors | Lue, N.,Sharma, A.,Mondragon, A.,Wang, J.C. (deposition date: 1996-09-14, release date: 1997-03-12, Last modification date: 2024-02-14) |
Primary citation | Lue, N.,Sharma, A.,Mondragon, A.,Wang, J.C. A 26 kDa yeast DNA topoisomerase I fragment: crystallographic structure and mechanistic implications. Structure, 3:1315-1322, 1995 Cited by PubMed Abstract: Type I DNA topoisomerases, divided mechanistically into two subfamilies, are ubiquitous enzymes that participate in replication and transcription. In addition to its role in these fundamental processes, the biological importance of eukaryotic DNA topoisomerase I is underscored by its identification as the target of the antitumor alkaloid camptothecin. An understanding of the mechanism of catalysis and interactions with camptothecin and other drugs has been hampered by a lack of detailed structural information. PubMed: 8747458DOI: 10.1016/S0969-2126(01)00269-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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